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1HSA

THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC

Summary for 1HSA
Entry DOI10.2210/pdb1hsa/pdb
DescriptorCLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-B*2705), BETA 2-MICROGLOBULIN, MODEL PEPTIDE SEQUENCE - ARAAAAAAA, ... (4 entities in total)
Functional Keywordshistocompatibility antigen
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P03989
Secreted: P61769
Total number of polymer chains6
Total formula weight88840.30
Authors
Madden, D.R.,Gorga, J.C.,Strominger, J.L.,Wiley, D.C. (deposition date: 1992-08-11, release date: 1992-10-15, Last modification date: 2011-07-13)
Primary citationMadden, D.R.,Gorga, J.C.,Strominger, J.L.,Wiley, D.C.
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC.
Cell(Cambridge,Mass.), 70:1035-1048, 1992
Cited by
PubMed: 1525820
DOI: 10.1016/0092-8674(92)90252-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

217705

数据于2024-03-27公开中

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