B2M
Synonyms
HDCMA22P, CDABP0092, B2M, Beta-2-Microglobulin, Beta Chain Of MHC Class I Molecules, Beta-2-Microglobin, IMD43, beta 2-Microglobulin
Description
Beta 2-microglobulin (B2M) is a component of the major histocompatibility complex (MHC) class I molecule, which presents tumor antigens to T lymphocytes to trigger cancer cell destruction.Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation.
KO Status
F0
Drug Information
Drug Name
Code
Phase
Company
Indications
Clinical Trials
R7V therapeutic antibody program (URRMA Biopharma/Dyax)
Discontinued
Urrma Biopharma, Dyax Corp
HIV Infections
References
Title
Authors
Source
High-resolution crystal structure of beta2-microglobulin formed at pH 7.0
Iwata K., Matsuura T., Sakurai K., Nakagawa A., Goto Y.,
J. Biochem. 142:413-419(2007)
DE loop mutations affect beta2-microglobulin stability and amyloid aggregation
Ricagno S., Colombo M., de Rosa M., Sangiovanni E., Giorgetti S., Raimondi S., Bellotti V., Bolognesi M.,
Biochem. Biophys. Res. Commun. 377:146-150(2008)
The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties
Esposito G., Ricagno S., Corazza A., Rennella E., Guemral D., Mimmi M.C., Betto E., Pucillo C.E., Fogolari F., Viglino P., Raimondi S., Giorgetti S., Bolognesi B., Merlini G., Stoppini M., Bolognesi M., Bellotti V.,
J. Mol. Biol. 378:887-897(2008)
Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation
Ricagno S., Raimondi S., Giorgetti S., Bellotti V., Bolognesi M.,
Biochem. Biophys. Res. Commun. 380:543-547(2009)
T-cell activation by transitory neo-antigens derived from distinct microbial pathways
Corbett A.J., Eckle S.B., Birkinshaw R.W., Liu L., Patel O., Mahony J., Chen Z., Reantragoon R., Meehan B., Cao H., Williamson N.A., Strugnell R.A., Van Sinderen D., Mak J.Y., Fairlie D.P., Kjer-Nielsen L., Rossjohn J., McCluskey J.,
Nature 509:361-365(2014)
Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant beta2-microglobulin gene
Wani M.A., Haynes L.D., Kim J., Bronson C.L., Chaudhury C., Mohanty S., Waldmann T.A., Robinson J.M., Anderson C.L.,
Proc. Natl. Acad. Sci. U.S.A. 103:5084-5089(2006)
Amino acid sequence of a modified beta 2-microglobulin in renal failure patient urine and long-term dialysis patient blood
Momoi T., Suzuki M., Titani K., Hisanaga S., Ogawa H., Saito A.,
Clin. Chim. Acta 236:135-144(1995)
Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., Suarez T., Elortza F.,
J. Proteome Res. 14:2649-2658(2015)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.,
J. Proteomics 96:253-262(2014)
N-terminome analysis of the human mitochondrial proteome
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.,
Proteomics 15:2519-2524(2015)
TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide
Braud V.M., Allan D.S., Wilson D., McMichael A.J.,
Curr. Biol. 8:1-10(1998)
Complete sequencing and characterization of 21,243 full-length human cDNAs
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Sugano S.,
Nat. Genet. 36:40-45(2004)
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)
The MGC Project Team,
Genome Res. 14:2121-2127(2004)
The beta-2-microglobulin mRNA in human Daudi cells has a mutated initiation codon but is still inducible by interferon
Rosa F., Berissi H., Weissenbach J., Maroteaux L., Fellous M., Revel M.,
EMBO J. 2:239-243(1983)
Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human beta 2-microglobulin
Suggs S.V., Wallace R.B., Hirose T., Kawashima E.H., Itakura K.,
Proc. Natl. Acad. Sci. U.S.A. 78:6613-6617(1981)
The complete amino acid sequence of beta 2-microglobulin
Cunningham B.A., Wang J.L., Berggard I., Peterson P.A.,
Biochemistry 12:4811-4822(1973)
Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis
Gorevic P.D., Munoz P.C., Casey T.T., DiRaimondo C.R., Stone W.J., Prelli F.C., Rodrigues M.M., Poulik M.D., Frangione B.,
Proc. Natl. Acad. Sci. U.S.A. 83:7908-7912(1986)
Biochemical characterization of serum and urinary beta 2 microglobulin in end-stage renal disease patients
Argiles A., Derancourt J., Jauregui-Adell J., Mion C., Demaille J.G.,
Nephrol. Dial. Transplant. 7:1106-1110(1992)
Isolation of a granulocyte inhibitory protein from uraemic patients with homology of beta 2-microglobulin
Haag-Weber M., Mai B., Hoerl W.H.,
Nephrol. Dial. Transplant. 9:382-388(1994)
HLA-F is a predominantly empty, intracellular, TAP-associated MHC class Ib protein with a restricted expression pattern
Wainwright S.D., Biro P.A., Holmes C.H.,
J. Immunol. 164:319-328(2000)
The ESAT-6 protein of Mycobacterium tuberculosis interacts with beta-2-microglobulin (beta2M) affecting antigen presentation function of macrophage
Sreejit G., Ahmed A., Parveen N., Jha V., Valluri V.L., Ghosh S., Mukhopadhyay S.,
PLoS Pathog. 10:E1004446-E1004446(2014)
Glycation of human beta 2-microglobulin in patients with hemodialysis-associated amyloidosis: identification of the glycated sites
Miyata T., Inagi R., Wada Y., Ueda Y., Iida Y., Takahashi M., Taniguchi N., Maeda K.,
Biochemistry 33:12215-12221(1994)
Initial characterization of the human central proteome
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.,
BMC Syst. Biol. 5:17-17(2011)
Hereditary systemic amyloidosis due to Asp76Asn variant beta2-microglobulin
Valleix S., Gillmore J.D., Bridoux F., Mangione P.P., Dogan A., Nedelec B., Boimard M., Touchard G., Goujon J.M., Lacombe C., Lozeron P., Adams D., Lacroix C., Maisonobe T., Plante-Bordeneuve V., Vrana J.A., Theis J.D., Giorgetti S., Bellotti V.,
N. Engl. J. Med. 366:2276-2283(2012)
Structure of the human class I histocompatibility antigen, HLA-A2
Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., Wiley D.C.,
Nature 329:506-512(1987)
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6-A resolution
Saper M.A., Bjorkman P.J., Wiley D.C.,
J. Mol. Biol. 219:277-319(1991)
1H NMR assignments and secondary structure of human beta 2-microglobulin in solution
Okon M., Bray P., Vucelic D.,
Biochemistry 31:8906-8915(1992)
The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain
Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.,
Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995)
The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit
Guessow D., Rein R., Ginjaar I., Hochstenbach F., Seemann G., Kottman A., Ploegh H.L.,
J. Immunol. 139:3132-3138(1987)
Cloning of human beta-microglobulin gene and its high expression in Escherichia coli
He X.H., Xu L.H., Liu Y., Zeng Y.Y.,
Sheng Wu Gong Cheng Xue Bao 20:99-103(2004)
Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53
Smith K.J., Reid S.W., Harlos K., McMichael A.J., Stuart D.I., Bell J.I., Jones E.Y.,
Immunity 4:215-228(1996)
Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties
Trinh C.H., Smith D.P., Kalverda A.P., Phillips S.E., Radford S.E.,
Proc. Natl. Acad. Sci. U.S.A. 99:9771-9776(2002)
A structural basis for immunodominant human T cell receptor recognition
Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.,
Nat. Immunol. 4:657-663(2003)
Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis
Kihara M., Chatani E., Iwata K., Yamamoto K., Matsuura T., Nakagawa A., Naiki H., Goto Y.,
J. Biol. Chem. 281:31061-31069(2006)
A native to amyloidogenic transition regulated by a backbone trigger
Eakin C.M., Berman A.J., Miranker A.D.,
Nat. Struct. Mol. Biol. 13:202-208(2006)
Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)
Shiroishi M., Kuroki K., Rasubala L., Tsumoto K., Kumagai I., Kurimoto E., Kato K., Kohda D., Maenaka K.,
Proc. Natl. Acad. Sci. U.S.A. 103:16412-16417(2006)
The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit.
Guessow D., Rein R., Ginjaar I., Hochstenbach F., Seemann G., Kottman A., Ploegh H.L.,
J. Immunol. 139:3132-3138(1987)
Cloning of human beta-microglobulin gene and its high expression in Escherichia coli.
He X.H., Xu L.H., Liu Y., Zeng Y.Y.,
Sheng Wu Gong Cheng Xue Bao 20:99-103(2004)
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Sugano S.,
Nat. Genet. 36:40-45(2004)
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team,
Genome Res. 14:2121-2127(2004)
The beta-2-microglobulin mRNA in human Daudi cells has a mutated initiation codon but is still inducible by interferon.
Rosa F., Berissi H., Weissenbach J., Maroteaux L., Fellous M., Revel M.,
EMBO J. 2:239-243(1983)
Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human beta 2-microglobulin.
Suggs S.V., Wallace R.B., Hirose T., Kawashima E.H., Itakura K.,
Proc. Natl. Acad. Sci. U.S.A. 78:6613-6617(1981)
The complete amino acid sequence of beta 2-microglobulin.
Cunningham B.A., Wang J.L., Berggard I., Peterson P.A.,
Biochemistry 12:4811-4822(1973)
Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.
Gorevic P.D., Munoz P.C., Casey T.T., DiRaimondo C.R., Stone W.J., Prelli F.C., Rodrigues M.M., Poulik M.D., Frangione B.,
Proc. Natl. Acad. Sci. U.S.A. 83:7908-7912(1986)
Biochemical characterization of serum and urinary beta 2 microglobulin in end-stage renal disease patients.
Argiles A., Derancourt J., Jauregui-Adell J., Mion C., Demaille J.G.,
Nephrol. Dial. Transplant. 7:1106-1110(1992)
Isolation of a granulocyte inhibitory protein from uraemic patients with homology of beta 2-microglobulin.
Haag-Weber M., Mai B., Hoerl W.H.,
Nephrol. Dial. Transplant. 9:382-388(1994)
Amino acid sequence of a modified beta 2-microglobulin in renal failure patient urine and long-term dialysis patient blood.
Momoi T., Suzuki M., Titani K., Hisanaga S., Ogawa H., Saito A.,
Clin. Chim. Acta 236:135-144(1995)
Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification.
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., Suarez T., Elortza F.,
J. Proteome Res. 14:2649-2658(2015)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.,
J. Proteomics 96:253-262(2014)
N-terminome analysis of the human mitochondrial proteome.
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.,
Proteomics 15:2519-2524(2015)
TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide.
Braud V.M., Allan D.S., Wilson D., McMichael A.J.,
Curr. Biol. 8:1-10(1998)
HLA-F is a predominantly empty, intracellular, TAP-associated MHC class Ib protein with a restricted expression pattern.
Wainwright S.D., Biro P.A., Holmes C.H.,
J. Immunol. 164:319-328(2000)
The ESAT-6 protein of Mycobacterium tuberculosis interacts with beta-2-microglobulin (beta2M) affecting antigen presentation function of macrophage.
Sreejit G., Ahmed A., Parveen N., Jha V., Valluri V.L., Ghosh S., Mukhopadhyay S.,
PLoS Pathog. 10:E1004446-E1004446(2014)
Glycation of human beta 2-microglobulin in patients with hemodialysis-associated amyloidosis: identification of the glycated sites.
Miyata T., Inagi R., Wada Y., Ueda Y., Iida Y., Takahashi M., Taniguchi N., Maeda K.,
Biochemistry 33:12215-12221(1994)
Initial characterization of the human central proteome.
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.,
BMC Syst. Biol. 5:17-17(2011)
Hereditary systemic amyloidosis due to Asp76Asn variant beta2-microglobulin.
Valleix S., Gillmore J.D., Bridoux F., Mangione P.P., Dogan A., Nedelec B., Boimard M., Touchard G., Goujon J.M., Lacombe C., Lozeron P., Adams D., Lacroix C., Maisonobe T., Plante-Bordeneuve V., Vrana J.A., Theis J.D., Giorgetti S., Bellotti V.,
N. Engl. J. Med. 366:2276-2283(2012)
Structure of the human class I histocompatibility antigen, HLA-A2.
Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., Wiley D.C.,
Nature 329:506-512(1987)
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6-A resolution.
Saper M.A., Bjorkman P.J., Wiley D.C.,
J. Mol. Biol. 219:277-319(1991)
1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
Okon M., Bray P., Vucelic D.,
Biochemistry 31:8906-8915(1992)
The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain.
Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.,
Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995)
Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.
Smith K.J., Reid S.W., Harlos K., McMichael A.J., Stuart D.I., Bell J.I., Jones E.Y.,
Immunity 4:215-228(1996)
Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties.
Trinh C.H., Smith D.P., Kalverda A.P., Phillips S.E., Radford S.E.,
Proc. Natl. Acad. Sci. U.S.A. 99:9771-9776(2002)
A structural basis for immunodominant human T cell receptor recognition.
Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.,
Nat. Immunol. 4:657-663(2003)
Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis.
Kihara M., Chatani E., Iwata K., Yamamoto K., Matsuura T., Nakagawa A., Naiki H., Goto Y.,
J. Biol. Chem. 281:31061-31069(2006)
A native to amyloidogenic transition regulated by a backbone trigger.
Eakin C.M., Berman A.J., Miranker A.D.,
Nat. Struct. Mol. Biol. 13:202-208(2006)
Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d).
Shiroishi M., Kuroki K., Rasubala L., Tsumoto K., Kumagai I., Kurimoto E., Kato K., Kohda D., Maenaka K.,
Proc. Natl. Acad. Sci. U.S.A. 103:16412-16417(2006)
High-resolution crystal structure of beta2-microglobulin formed at pH 7.0.
Iwata K., Matsuura T., Sakurai K., Nakagawa A., Goto Y.,
J. Biochem. 142:413-419(2007)
DE loop mutations affect beta2-microglobulin stability and amyloid aggregation.
Ricagno S., Colombo M., de Rosa M., Sangiovanni E., Giorgetti S., Raimondi S., Bellotti V., Bolognesi M.,
Biochem. Biophys. Res. Commun. 377:146-150(2008)
The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties.
Esposito G., Ricagno S., Corazza A., Rennella E., Guemral D., Mimmi M.C., Betto E., Pucillo C.E., Fogolari F., Viglino P., Raimondi S., Giorgetti S., Bolognesi B., Merlini G., Stoppini M., Bolognesi M., Bellotti V.,
J. Mol. Biol. 378:887-897(2008)
Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation.
Ricagno S., Raimondi S., Giorgetti S., Bellotti V., Bolognesi M.,
Biochem. Biophys. Res. Commun. 380:543-547(2009)
T-cell activation by transitory neo-antigens derived from distinct microbial pathways.
Corbett A.J., Eckle S.B., Birkinshaw R.W., Liu L., Patel O., Mahony J., Chen Z., Reantragoon R., Meehan B., Cao H., Williamson N.A., Strugnell R.A., Van Sinderen D., Mak J.Y., Fairlie D.P., Kjer-Nielsen L., Rossjohn J., McCluskey J.,
Nature 509:361-365(2014)
Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant beta2-microglobulin gene.
Wani M.A., Haynes L.D., Kim J., Bronson C.L., Chaudhury C., Mohanty S., Waldmann T.A., Robinson J.M., Anderson C.L.,
Proc. Natl. Acad. Sci. U.S.A. 103:5084-5089(2006)
Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity.
Glithero A., Tormo J., Haurum J.S., Arsequell G., Valencia G., Edwards J., Springer S., Townsend A., Pao Y.L., Wormald M., Dwek R.A., Jones E.Y., Elliott T.,
Immunity 10:63-74(1999)
Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.
Gross B.S., Lee J.R., Clements J.L., Turner M., Tybulewicz V.L., Findell P.R., Koretzky G.A., Watson S.P.,
J Biol Chem 274:5963-5971(1999)
Cell surface expression of HLA-E: interaction with human beta-2 microglobulin and allelic differences.
Ulbrecht M., Courturier A., Martinozzi S., Pla M., Srivastava R., Peterson P.A., Weiss E.H.,
Eur. J. Immunol. 29:537-547(1999)
A role for the adaptor protein LAT in human NK cell-mediated cytotoxicity.
Jevremovic D., Billadeau D.D., Schoon R.A., Dick C.J., Irvin B.J., Zhang W., Samelson L.E., Abraham R.T., Leibson P.J.,
J. Immunol. 162:2453-2456(1999)
A stop-codon mutation in the BRI gene associated with familial British dementia.
Vidal R., Frangione B., Rostagno A., Mead S., Revesz T., Plant G., Ghiso J.,
Nature 399:776-781(1999)
Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid.
Haeggqvist B., Naeslund J., Sletten K., Westermark G.T., Mucchiano G., Tjernberg L.O., Nordstedt C., Engstroem U., Westermark P.,
Proc. Natl. Acad. Sci. U.S.A. 96:8669-8674(1999)
Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor.
Fan Q.R., Wiley D.C.,
J Exp Med 190:113-123(1999)
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical.
Ding Y.H., Baker B.M., Garboczi D.N., Biddison W.E., Wiley D.C.,
Immunity 11:45-56(1999)
Recycling MHC class I molecules and endosomal peptide loading.
Gromme M., Uytdehaag F.G., Janssen H., Calafat J., van Binnendijk R.S., Kenter M.J., Tulp A., Verwoerd D., Neefjes J.,
Proc Natl Acad Sci U S A 96:10326-10331(1999)
Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth.
McLaurin J., Franklin T., Zhang X., Deng J., Fraser P.E.,
Eur J Biochem 266:1101-1110(1999)
Poor binding of a HER-2/neu epitope (GP2) to HLA-A2.1 is due to a lack of interactions with the center of the peptide.
Kuhns J.J., Batalia M.A., Yan S., Collins E.J.,
J. Biol. Chem. 274:36422-36427(1999)
The structural basis for the increased immunogenicity of two HIV-reverse transcriptase peptide variant/class I major histocompatibility complexes.
Kirksey T.J., Pogue-Caley R.R., Frelinger J.A., Collins E.J.,
J Biol Chem 274:37259-37264(1999)
Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold.
Wingren C., Crowley M.P., Degano M., Chien Y., Wilson I.A.,
Science 287:310-314(2000)
Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor.
Bennett M.J., Lebron J.A., Bjorkman P.J.,
Nature 403:46-53(2000)
COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites.
Stephens D.J., Lin-Marq N., Pagano A., Pepperkok R., Paccaud J.P.,
J Cell Sci 113:2177-2185(2000)
The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site.
Khan A.R., Baker B.M., Ghosh P., Biddison W.E., Wiley D.C.,
J Immunol 164:6398-6405(2000)
Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand.
Boyington J.C., Motyka S.A., Schuck P., Brooks A.G., Sun P.D.,
Nature 405:537-543(2000)
Identification of NY-ESO-1 peptide analogues capable of improved stimulation of tumor-reactive CTL.
Chen J.L., Dunbar P.R., Gileadi U., Jager E., Gnjatic S., Nagata Y., Stockert E., Panicali D.L., Chen Y.T., Knuth A., Old L.J., Cerundolo V.,
J Immunol 165:948-955(2000)
Direct selection of a human antibody fragment directed against the tumor T-cell epitope HLA-A1-MAGE-A1 from a nonimmunized phage-Fab library.
Chames P., Hufton S.E., Coulie P.G., Uchanska-Ziegler B., Hoogenboom H.R.,
Proc Natl Acad Sci U S A 97:7969-7974(2000)
Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor.
West A.P. Jr., Bjorkman P.J.,
Biochemistry 39:9698-9708(2000)
Nonstandard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes.
Maenaka K., Maenaka T., Tomiyama H., Takiguchi M., Stuart D.I., Jones E.Y.,
J Immunol 165:3260-3267(2000)
Dynamics of transitional endoplasmic reticulum sites in vertebrate cells.
Hammond A.T., Glick B.S.,
Mol Biol Cell 11:3013-3030(2000)
Selective export of MHC class I molecules from the ER after their dissociation from TAP.
Spiliotis E.T., Manley H., Osorio M., Zuniga M.C., Edidin M.,
Immunity 13:841-851(2000)
Antigen loading of MHC class I molecules in the endocytic tract.
Kleijmeer M.J., Escola J.M., UytdeHaag F.G., Jakobson E., Griffith J.M., Osterhaus A.D., Stoorvogel W., Melief C.J., Rabouille C., Geuze H.J.,
Traffic 2:124-137(2001)
Class I major histocompatibility complex anchor substitutions alter the conformation of T cell receptor contacts.
Sharma A.K., Kuhns J.J., Yan S., Friedline R.H., Long B., Tisch R., Collins E.J.,
J Biol Chem 276:21443-21449(2001)
Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex.
Fan Q.R., Long E.O., Wiley D.C.,
Nat. Immunol. 2:452-460(2001)
Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells.
Paz P.E., Wang S., Clarke H., Lu X., Stokoe D., Abo A.,
Biochem. J. 356:461-471(2001)
Antigen presentation subverted: structure of the human cytomegalovirus protein US2 bound to the class I molecule HLA-A2.
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