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3BVN

High resolution crystal structure of HLA-B*1402 in complex with the latent membrane protein 2 peptide (LMP2) of Epstein-Barr virus

Summary for 3BVN
Entry DOI10.2210/pdb3bvn/pdb
Related1UXS
DescriptorHLA class I histocompatibility antigen, B*1402 alpha chain, Beta-2-microglobulin, Latent membrane protein 2 peptide, ... (4 entities in total)
Functional Keywordsmajor histocompatibility complex, mhc, human leukocyte antigen, hla, hla-b14, hla-b*14, hla-b1402, hla-b*1402, plmp2, ankylosing spondylitis, disease mutation, glycation, glycoprotein, immune response, immunoglobulin domain, mhc i, pyrrolidone carboxylic acid, secreted, alternative splicing, cytoplasm, host-virus interaction, membrane, phosphoprotein, transmembrane, ubl conjugation, immune system
Biological sourceHomo sapiens (Human)
More
Cellular locationSecreted: P61769
Isoform LMP2A: Host cell membrane; Multi- pass membrane protein. Isoform LMP2B: Host endomembrane system; Multi-pass membrane protein: P13285
Total number of polymer chains6
Total formula weight90710.59
Authors
Kumar, P.,Vahedi-Faridi, A.,Saenger, W.,Uchanska-Ziegler, B.,Ziegler, A. (deposition date: 2008-01-07, release date: 2009-02-03, Last modification date: 2023-08-30)
Primary citationKumar, P.,Vahedi-Faridi, A.,Saenger, W.,Merino, E.,Lopez de Castro, J.A.,Uchanska-Ziegler, B.,Ziegler, A.
Structural basis for T cell alloreactivity among three HLA-B14 and HLA-B27 antigens
J.Biol.Chem., 284:29784-29797, 2009
Cited by
PubMed: 19617632
DOI: 10.1074/jbc.M109.038497
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

217705

数据于2024-03-27公开中

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