5VGD
Crystal Structure of HLA-C*0501 in complex with SAE
Summary for 5VGD
| Entry DOI | 10.2210/pdb5vgd/pdb |
| Related | 5vge |
| Descriptor | HLA class I histocompatibility antigen, Cw-5 alpha chain, Beta-2-microglobulin, SER-ALA-GLU-PRO-VAL-PRO-LEU-GLN-LEU, ... (4 entities in total) |
| Functional Keywords | hla, immune system, hla-c |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Membrane; Single-pass type I membrane protein: Q9TNN7 Secreted . Note=(Microbial infection) In the presence of M: P61769 |
| Total number of polymer chains | 3 |
| Total formula weight | 44936.84 |
| Authors | Gras, S.,Rossjohn, J. (deposition date: 2017-04-11, release date: 2017-05-31, Last modification date: 2024-10-16) |
| Primary citation | Kaur, G.,Gras, S.,Mobbs, J.I.,Vivian, J.P.,Cortes, A.,Barber, T.,Kuttikkatte, S.B.,Jensen, L.T.,Attfield, K.E.,Dendrou, C.A.,Carrington, M.,McVean, G.,Purcell, A.W.,Rossjohn, J.,Fugger, L. Structural and regulatory diversity shape HLA-C protein expression levels. Nat Commun, 8:15924-15924, 2017 Cited by PubMed Abstract: Expression of HLA-C varies widely across individuals in an allele-specific manner. This variation in expression can influence efficacy of the immune response, as shown for infectious and autoimmune diseases. MicroRNA binding partially influences differential HLA-C expression, but the additional contributing factors have remained undetermined. Here we use functional and structural analyses to demonstrate that HLA-C expression is modulated not just at the RNA level, but also at the protein level. Specifically, we show that variation in exons 2 and 3, which encode the α1/α2 domains, drives differential expression of HLA-C allomorphs at the cell surface by influencing the structure of the peptide-binding cleft and the diversity of peptides bound by the HLA-C molecules. Together with a phylogenetic analysis, these results highlight the diversity and long-term balancing selection of regulatory factors that modulate HLA-C expression. PubMed: 28649982DOI: 10.1038/ncomms15924 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.32 Å) |
Structure validation
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