3mrd
From Proteopedia
(Difference between revisions)
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<StructureSection load='3mrd' size='340' side='right' caption='[[3mrd]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3mrd' size='340' side='right' caption='[[3mrd]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3mrd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3mrd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRD FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mr9|3mr9]], [[3mrb|3mrb]], [[3mrc|3mrc]], [[3mre|3mre]], [[3mrf|3mrf]], [[3mrg|3mrg]], [[3mrh|3mrh]], [[3mri|3mri]], [[3mrj|3mrj]], [[3mrk|3mrk]], [[3mrl|3mrl]], [[3mrm|3mrm]], [[3mrn|3mrn]], [[3mro|3mro]], [[3mrp|3mrp]], [[3mrq|3mrq]], [[3mrr|3mrr]], [[3gsn|3gsn]], [[3gso|3gso]], [[3gsq|3gsq]], [[3gsr|3gsr]], [[3gsu|3gsu]], [[3gsv|3gsv]], [[3gsw|3gsw]], [[3gsx|3gsx]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mr9|3mr9]], [[3mrb|3mrb]], [[3mrc|3mrc]], [[3mre|3mre]], [[3mrf|3mrf]], [[3mrg|3mrg]], [[3mrh|3mrh]], [[3mri|3mri]], [[3mrj|3mrj]], [[3mrk|3mrk]], [[3mrl|3mrl]], [[3mrm|3mrm]], [[3mrn|3mrn]], [[3mro|3mro]], [[3mrp|3mrp]], [[3mrq|3mrq]], [[3mrr|3mrr]], [[3gsn|3gsn]], [[3gso|3gso]], [[3gsq|3gsq]], [[3gsr|3gsr]], [[3gsu|3gsu]], [[3gsv|3gsv]], [[3gsw|3gsw]], [[3gsx|3gsx]]</td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA, HLA-A, HLAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA, HLA-A, HLAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), B2M, BETA-2 MICROGLUBULIN, CDABP0092, HDCMA22P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3mrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrd RCSB], [http://www.ebi.ac.uk/pdbsum/3mrd PDBsum]</span></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=3mrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrd RCSB], [http://www.ebi.ac.uk/pdbsum/3mrd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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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> | [[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 == | == Function == | ||
- | [[http://www.uniprot.org/uniprot/1A02_HUMAN 1A02_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. | + | [[http://www.uniprot.org/uniprot/1A02_HUMAN 1A02_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/PP65_HCMVM PP65_HCMVM]] Counteracts the host antiviral immune response by preventing IRF3 from entering the nucleus once activated and phosphorylated. Participates also in the transactivation of viral major immediate-early genes by recruiting host IFI16 to their promoters. [[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. |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structural rules governing peptide/MHC (pMHC) recognition by T cells remain unclear. To address this question, we performed a structural characterization of several HLA-A2/peptide complexes and assessed in parallel their antigenicity, by analyzing the frequency of the corresponding Ag-specific naive T cells in A2(+) and A2(-) individuals, as well as within CD4(+) and CD8(+) subsets. We were able to find a correlation between specific naive T cell frequency and peptide solvent accessibility and/or mobility for a subset of moderately prominent peptides. However, one single structural parameter of the pMHC complexes could not be identified to explain each peptide antigenicity. Enhanced pMHC antigenicity was associated with both highly biased TRAV usage, possibly reflecting favored interaction between particular pMHC complexes and germline TRAV loops, and peptide structural features allowing interactions with a broad range of permissive CDR3 loops. In this context of constrained TCR docking mode, an optimal peptide solvent exposed surface leading to an optimal complementarity with TCR interface may constitute one of the key features leading to high frequency of specific T cells. Altogether our results suggest that frequency of specific T cells depends on the fine-tuning of several parameters, the structural determinants governing TCR-pMHC interaction being just one of them. | ||
+ | |||
+ | Analysis of relationships between peptide/MHC structural features and naive T cell frequency in humans.,Reiser JB, Legoux F, Gras S, Trudel E, Chouquet A, Leger A, Le Gorrec M, Machillot P, Bonneville M, Saulquin X, Housset D J Immunol. 2014 Dec 15;193(12):5816-26. doi: 10.4049/jimmunol.1303084. Epub 2014 , Nov 12. PMID:25392532<ref>PMID:25392532</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Human]] |
[[Category: Bonneville, M]] | [[Category: Bonneville, M]] | ||
[[Category: Chouquet, A]] | [[Category: Chouquet, A]] |
Revision as of 11:01, 28 January 2015
Crystal Structure of MHC class I HLA-A2 molecule complexed with HCMV pp65-495-503 nonapeptide V6G variant
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Categories: Human | Bonneville, M | Chouquet, A | Debeaupuis, E | Echasserieau, K | Gras, S | Housset, D | Reiser, J B | Saulquin, X | Cytomegalovirus | Hla | Immune response | Immune system | Mhc class i | Nonapeptide | Pp65 protein | Viral peptide