4prb
From Proteopedia
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- | {{STRUCTURE_4prb| PDB=4prb | SCENE= }} | ||
- | ===Crystal structure of a HLA-B*35:08-HPVG-A4=== | ||
- | == | + | ==Crystal structure of a HLA-B*35:08-HPVG-A4== |
- | [[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN | + | <StructureSection load='4prb' size='340' side='right'caption='[[4prb]], [[Resolution|resolution]] 1.75Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4prb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Epstein-barr_virus_strain_ag876 Epstein-barr virus strain ag876] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PRB FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4prb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4prb OCA], [https://pdbe.org/4prb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4prb RCSB], [https://www.ebi.ac.uk/pdbsum/4prb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4prb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref> Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Mutations within T cell epitopes represent a common mechanism of viral escape from the host protective immune response. The diverse T cell repertoire and the extensive human leukocyte antigen (HLA) polymorphism across populations is the evolutionary response to viral mutation. However, the molecular basis underpinning the interplay between HLA polymorphism, the T cell repertoire, and viral escape is unclear. Here we investigate the T cell response to a HLA-B*35:01- and HLA-B*35:08-restricted 407HPVGEADYFEY417 epitope from Epstein-Barr virus and naturally occurring variants at positions 4 and 5 thereof. Each viral variant differently impacted on the epitope's flexibility and conformation when bound to HLA-B*35:08 or HLA-B*35:01. We provide a molecular basis for understanding how the single residue polymorphism that discriminates between HLA-B*35:01/08 profoundly impacts on T cell receptor recognition. Surprisingly, one viral variant (P5-Glu to P5-Asp) effectively changed restriction preference from HLA-B*35:01 to HLA-B*35:08. Collectively, our study portrays the interplay between the T cell response, viral escape, and HLA polymorphism, whereby HLA polymorphism enables altered presentation of epitopes from different strains of Epstein-Barr virus. | ||
- | + | A Molecular Basis for the Interplay between T Cells, Viral Mutants, and Human Leukocyte Antigen Micropolymorphism.,Liu YC, Chen Z, Neller MA, Miles JJ, Purcell AW, McCluskey J, Burrows SR, Rossjohn J, Gras S J Biol Chem. 2014 Jun 13;289(24):16688-16698. Epub 2014 Apr 23. PMID:24759101<ref>PMID:24759101</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
+ | <div class="pdbe-citations 4prb" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |
- | [[ | + | *[[MHC 3D structures|MHC 3D structures]] |
- | [[ | + | *[[MHC I 3D structures|MHC I 3D structures]] |
- | [[ | + | == References == |
- | + | <references/> | |
- | [[Category: Epstein-barr virus]] | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Epstein-barr virus strain ag876]] |
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Gras S]] |
+ | [[Category: Rossjohn J]] | ||
+ | [[Category: Yu Chih L]] |
Current revision
Crystal structure of a HLA-B*35:08-HPVG-A4
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