1UVQ
Crystal structure of HLA-DQ0602 in complex with a hypocretin peptide
Summary for 1UVQ
Entry DOI | 10.2210/pdb1uvq/pdb |
Descriptor | HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, OREXIN, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
Functional Keywords | immunology, mhc class ii, diabetes, narcolepsy, autoimmune disease, structural proteomics in europe, spine, structural genomics, immune system |
Biological source | HOMO SAPIENS (HUMAN) More |
Total number of polymer chains | 3 |
Total formula weight | 49785.54 |
Authors | Siebold, C.,Hansen, B.E.,Wyer, J.R.,Harlos, K.,Esnouf, R.E.,Svejgaard, A.,Bell, J.I.,Strominger, J.L.,Jones, E.Y.,Fugger, L. (deposition date: 2004-01-22, release date: 2004-02-05, Last modification date: 2024-10-23) |
Primary citation | Siebold, C.,Hansen, B.E.,Wyer, J.R.,Harlos, K.,Esnouf, R.E.,Svejgaard, A.,Bell, J.I.,Strominger, J.L.,Jones, E.Y.,Fugger, L. Crystal Structure of Hla-Dq0602 that Protects Against Type 1 Diabetes and Confers Strong Susceptibility to Narcolepsy Proc.Natl.Acad.Sci.USA, 101:1999-, 2004 Cited by PubMed Abstract: The MHC class II molecule DQ0602 confers strong susceptibility to narcolepsy but dominant protection against type 1 diabetes. The crystal structure of DQ0602 reveals the molecular features underlying these contrasting genetic properties. Structural comparisons to homologous DQ molecules with differential disease associations highlight a previously unrecognized interplay between the volume of the P6 pocket and the specificity of the P9 pocket, which implies that presentation of an expanded peptide repertoire is critical for dominant protection against type 1 diabetes. In narcolepsy, the volume of the P4 pocket appears central to the susceptibility, suggesting that the presentation of a specific peptide population plays a major role. PubMed: 14769912DOI: 10.1073/PNAS.0308458100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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