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6mtl

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m (Protected "6mtl" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6mtl is ON HOLD until Paper Publication
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==Crystal Structure of HLA-B*44:05 in complex with NP338 influenza peptide==
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<StructureSection load='6mtl' size='340' side='right' caption='[[6mtl]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6mtl]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MTL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mtl OCA], [http://pdbe.org/6mtl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mtl RCSB], [http://www.ebi.ac.uk/pdbsum/6mtl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mtl ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://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>
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== Function ==
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[[http://www.uniprot.org/uniprot/A0A0B7MGD5_HUMAN A0A0B7MGD5_HUMAN]] Involved in the presentation of foreign antigens to the immune system.[SAAS:SAAS00291881] [[http://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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Newly-emerged and vaccine-mismatched influenza A viruses (IAVs) result in a rapid global spread of the virus due to minimal antibody-mediated immunity. In that case, established CD8(+) T-cells can reduce disease severity. However, as mutations occur sporadically within immunogenic IAV-derived T-cell peptides, understanding of T-cell receptor (TCRalphabeta) cross-reactivity towards IAV variants is needed for a vaccine design. Here, we investigate TCRalphabeta cross-strain recognition across IAV variants within two immunodominant human IAV-specific CD8(+) T-cell epitopes, HLA-B*37:01-restricted NP338-346 (B37-NP338) and HLA-A*01:01-restricted NP44-52 (A1-NP44). We find high abundance of cross-reactive TCRalphabeta clonotypes recognizing distinct IAV variants. Structures of the wild-type and variant peptides revealed preserved conformation of the bound peptides. Structures of a cross-reactive TCR-HLA-B37-NP338 complex suggest that the conserved conformation of the variants underpins TCR cross-reactivity. Overall, cross-reactive CD8(+) T-cell responses, underpinned by conserved epitope structure, facilitates recognition of distinct IAV variants, thus CD8(+) T-cell-targeted vaccines could provide protection across different IAV strains.
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Authors:
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Broad CD8(+) T cell cross-recognition of distinct influenza A strains in humans.,Grant EJ, Josephs TM, Loh L, Clemens EB, Sant S, Bharadwaj M, Chen W, Rossjohn J, Gras S, Kedzierska K Nat Commun. 2018 Dec 21;9(1):5427. doi: 10.1038/s41467-018-07815-5. PMID:30575715<ref>PMID:30575715</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6mtl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gras, S]]
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[[Category: Cd8 t cell]]
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[[Category: Hla]]
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[[Category: Hla-b18]]
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[[Category: Hla-b37]]
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[[Category: Hla-b44]]
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[[Category: Immune system]]
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[[Category: Influenza]]
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[[Category: T cell]]
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[[Category: Tcr]]
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[[Category: Viral mutation]]

Revision as of 09:35, 13 February 2019

Crystal Structure of HLA-B*44:05 in complex with NP338 influenza peptide

6mtl, resolution 1.35Å

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