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 DOI | 10.2210/pdb1hsa/pdb |
Descriptor | CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-B*2705), BETA 2-MICROGLOBULIN, MODEL PEPTIDE SEQUENCE - ARAAAAAAA, ... (4 entities in total) |
Functional Keywords | histocompatibility antigen |
Biological source | Homo sapiens (human) More |
Cellular location | Membrane; Single-pass type I membrane protein: P03989 Secreted: P61769 |
Total number of polymer chains | 6 |
Total formula weight | 88840.30 |
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: 2024-06-05) |
Primary citation | Madden, 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: 1525820DOI: 10.1016/0092-8674(92)90252-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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