3lkp
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal Structure of HLA B*3501 in complex with influenza NP418 epitope from 1972 strain== | |
- | + | <StructureSection load='3lkp' size='340' side='right' caption='[[3lkp]], [[Resolution|resolution]] 1.80Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3lkp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LKP FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lkn|3lkn]], [[3lko|3lko]], [[3lkq|3lkq]], [[3lkr|3lkr]], [[3lks|3lks]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-B, HLAB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), B2M, CDABP0092, HDCMA22P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
+ | <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=3lkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lkp RCSB], [http://www.ebi.ac.uk/pdbsum/3lkp PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [[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> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/1B35_HUMAN 1B35_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[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. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lk/3lkp_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Preexisting T-cell immunity directed at conserved viral regions promotes enhanced recovery from influenza virus infections, with there being some evidence of cross-protection directed at variable peptides. Strikingly, many of the immunogenic peptides derived from the current pandemic A(H1N1)-2009 influenza virus are representative of the catastrophic 1918 "Spanish flu" rather than more recent "seasonal" strains. We present immunological and structural analyses of cross-reactive CD8(+) T-cell-mediated immunity directed at a variable (although highly cross-reactive) immunodominant NP(418-426) peptide that binds to a large B7 family (HLA-B*3501/03/0702) found throughout human populations. Memory CD8(+) T-cell specificity was probed for 12 different NP(418) mutants that emerged over the 9 decades between the 1918 and 2009 pandemics. Although there is evidence of substantial cross-reactivity among seasonal NP(418) mutants, current memory T-cell profiles show no preexisting immunity to the 2009-NP(418) variant or the 1918-NP(418) variant. Natural infection with the A(H1N1)-2009 virus, however, elicits CD8(+) T cells specific for the 2009-NP(418) and 1918-NP(418) epitopes. This analysis points to the potential importance of cross-reactive T-cell populations that cover the possible spectrum of T-cell variants and suggests that the identification of key residues/motifs that elicit cross-reactive T-cell sets could facilitate the evolution of immunization protocols that provide a measure of protection against unpredicted pandemic influenza viruses. Thus, it is worth exploring the potential of vaccines that incorporate peptide variants with a proven potential for broader immunogenicity, especially to those that are not recognized by the current memory T-cell pool generated by exposure to influenza variants that cause successive seasonal epidemics. | ||
- | + | Cross-reactive CD8+ T-cell immunity between the pandemic H1N1-2009 and H1N1-1918 influenza A viruses.,Gras S, Kedzierski L, Valkenburg SA, Laurie K, Liu YC, Denholm JT, Richards MJ, Rimmelzwaan GF, Kelso A, Doherty PC, Turner SJ, Rossjohn J, Kedzierska K Proc Natl Acad Sci U S A. 2010 Jul 13;107(28):12599-604. Epub 2010 Jun 28. PMID:20616031<ref>PMID:20616031</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | ||
- | + | ||
- | + | ||
==See Also== | ==See Also== | ||
*[[Beta-2 microglobulin|Beta-2 microglobulin]] | *[[Beta-2 microglobulin|Beta-2 microglobulin]] | ||
*[[Major histocompatibility complex|Major histocompatibility complex]] | *[[Major histocompatibility complex|Major histocompatibility complex]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Denholm, J | + | [[Category: Denholm, J]] |
- | [[Category: Doherty, P C | + | [[Category: Doherty, P C]] |
- | [[Category: Gras, S | + | [[Category: Gras, S]] |
- | [[Category: Kedzierska, K | + | [[Category: Kedzierska, K]] |
- | [[Category: Kedzierski, L | + | [[Category: Kedzierski, L]] |
- | [[Category: Liu, Y C | + | [[Category: Liu, Y C]] |
- | [[Category: Richards, M | + | [[Category: Richards, M]] |
- | [[Category: Rimmelzwaan, G F | + | [[Category: Rimmelzwaan, G F]] |
- | [[Category: Rossjohn, J | + | [[Category: Rossjohn, J]] |
- | [[Category: Turner, S J | + | [[Category: Turner, S J]] |
- | [[Category: Valkenburg, S A | + | [[Category: Valkenburg, S A]] |
[[Category: Amyloid]] | [[Category: Amyloid]] | ||
[[Category: Amyloidosis]] | [[Category: Amyloidosis]] |
Revision as of 16:39, 18 December 2014
Crystal Structure of HLA B*3501 in complex with influenza NP418 epitope from 1972 strain
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Categories: Homo sapiens | Denholm, J | Doherty, P C | Gras, S | Kedzierska, K | Kedzierski, L | Liu, Y C | Richards, M | Rimmelzwaan, G F | Rossjohn, J | Turner, S J | Valkenburg, S A | Amyloid | Amyloidosis | Disease mutation | Disulfide bond | Glycation | Glycoprotein | Hla b*3501 | Host-virus interaction | Immune response | Immune system | Immunoglobulin domain | Influenza | Membrane | Mhc i | Np418 epitope | Pyrrolidone carboxylic acid | Secreted | Swine-flu | T cell immunity | Transmembrane