3skm

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<StructureSection load='3skm' size='340' side='right'caption='[[3skm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3skm' size='340' side='right'caption='[[3skm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3skm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SKM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3skm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SKM FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mi5|1mi5]], [[1kgc|1kgc]], [[1m05|1m05]], [[3ffc|3ffc]], [[3sjv|3sjv]], [[3skn|3skn]], [[3sko|3sko]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-B, HLAB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), B2M, CDABP0092, HDCMA22P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3skm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3skm OCA], [https://pdbe.org/3skm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3skm RCSB], [https://www.ebi.ac.uk/pdbsum/3skm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3skm ProSAT]</span></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=3skm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3skm OCA], [https://pdbe.org/3skm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3skm RCSB], [https://www.ebi.ac.uk/pdbsum/3skm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3skm ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[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 ==
== Function ==
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[[https://www.uniprot.org/uniprot/1B08_HUMAN 1B08_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[https://www.uniprot.org/uniprot/EBNA3_EBVG EBNA3_EBVG]] Plays an essential role for activation and immortalization of human B-cells. Represses transcription of viral promoters TP1 and Cp through interaction with host RBPJ, and inhibits EBNA2-mediated activation of these promoters. Since Cp is the promoter for all EBNA mRNAs, EBNA3A probably contributes to a negative autoregulatory control loop (By similarity). [[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.
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[https://www.uniprot.org/uniprot/EBNA3_EBVG EBNA3_EBVG] Plays an essential role for activation and immortalization of human B-cells. Represses transcription of viral promoters TP1 and Cp through interaction with host RBPJ, and inhibits EBNA2-mediated activation of these promoters. Since Cp is the promoter for all EBNA mRNAs, EBNA3A probably contributes to a negative autoregulatory control loop (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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EBV is a ubiquitous and persistent human pathogen, kept in check by the cytotoxic T cell response. In this study, we investigated how three TCRs, which differ in their T cell immunodominance hierarchies and gene usage, interact with the same EBV determinant (FLRGRAYGL), bound to the same Ag-presenting molecule, HLA-B8. We found that the three TCRs exhibit differing fine specificities for the viral Ag. Further, via structural and biophysical approaches, we demonstrated that the viral Ag provides the greatest energetic contribution to the TCR-peptide-HLA interaction, while focusing on a few adjacent HLA-based interactions to further tune fine-specificity requirements. Thus, the TCR engages the peptide-HLA with the viral Ag as the main glue, such that neighboring TCR-MHC interactions are recruited as a supportive adhesive. Collectively, we provide a portrait of how the host's adaptive immune response differentially engages a common viral Ag.
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A structural basis for varied alphabeta TCR usage against an immunodominant EBV antigen restricted to a HLA-B8 molecule.,Gras S, Wilmann PG, Chen Z, Halim H, Liu YC, Kjer-Nielsen L, Purcell AW, Burrows SR, McCluskey J, Rossjohn J J Immunol. 2012 Jan 1;188(1):311-21. Epub 2011 Dec 2. PMID:22140258<ref>PMID:22140258</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3skm" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Human gammaherpesvirus 4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Burrows, S R]]
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[[Category: Burrows SR]]
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[[Category: Chih, L Yu]]
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[[Category: Gras S]]
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[[Category: Gras, S]]
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[[Category: Hanim H]]
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[[Category: Hanim, H]]
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[[Category: Kjer-Nielsen L]]
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[[Category: Kjer-Nielsen, L]]
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[[Category: Mccluskey J]]
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[[Category: Mccluskey, J]]
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[[Category: Purcell AW]]
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[[Category: Purcell, A W]]
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[[Category: Rossjohn J]]
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[[Category: Rossjohn, J]]
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[[Category: Wilmann PG]]
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[[Category: Wilmann, P G]]
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[[Category: Yu Chih L]]
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[[Category: Zhenjun, C]]
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[[Category: Zhenjun C]]
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[[Category: Immune system]]
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[[Category: T cell receptor]]
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Revision as of 12:59, 14 March 2024

Crystal structure of the HLA-B8FLRGRAYVL, mutant G8V of the FLR peptide

PDB ID 3skm

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