3pqy: Difference between revisions
New page: '''Unreleased structure''' The entry 3pqy is ON HOLD Authors: Gras, S., Guillonneau, C., Turner, S.J., Rossjohn, J. Description: Crystal Structure of 6218 TCR in complex with the H2Db-... |
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==Crystal Structure of 6218 TCR in complex with the H2Db-PA224== | |||
<StructureSection load='3pqy' size='340' side='right'caption='[[3pqy]], [[Resolution|resolution]] 3.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pqy]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PQY 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]] 3.192Å</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=3pqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pqy OCA], [https://pdbe.org/3pqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pqy RCSB], [https://www.ebi.ac.uk/pdbsum/3pqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pqy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE] 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 == | |||
Pathogen-specific responses are characterized by preferred profiles of peptide+class I MHC (pMHCI) glycoprotein-specific T-cell receptor (TCR) Variable (V)-region use. How TCRV-region bias impacts TCRalphabeta heterodimer selection and resultant diversity is unclear. The D(b)PA(224)-specific TCR repertoire in influenza A virus-infected C57BL/6J (B6) mice exhibits a preferred TCRV-region bias toward the TRBV29 gene segment and an optimal complementarity determining region (CDR3) beta-length of 6 aa. Despite these restrictions, D(b)PA(224)-specific BV29(+) T cells use a wide array of unique CDR3beta sequences. Structural characterization of a single, TRBV29(+)D(b)P(A224)-specific TCRalphabeta-pMHCI complex demonstrated that CDR3alpha amino acid side chains made specific peptide interactions, but the CDR3beta main chain exclusively contacted peptides. Thus, length but not amino acid sequence was key for recognition and flexibility in Vbeta-region use. In support of this hypothesis, retrovirus expression of the D(b)PA(224)-specific TCRValpha-chain was used to constrain pairing within a naive/immune epitope-specific repertoire. The retrogenic TCRValpha paired with a diversity of CDR3betas in the context of a preferred TCRVbeta spectrum. Overall, these data provide an explanation for the combination of TCRV region bias and diversity within selected repertoires, even as they maintain exquisite pMHCI specificity. | |||
Structural basis for enabling T-cell receptor diversity within biased virus-specific CD8+ T-cell responses.,Day EB, Guillonneau C, Gras S, La Gruta NL, Vignali DA, Doherty PC, Purcell AW, Rossjohn J, Turner SJ Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9536-41. Epub 2011 May 23. PMID:21606376<ref>PMID:21606376</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3pqy" 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/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Gras S]] | |||
[[Category: Guillonneau C]] | |||
[[Category: Rossjohn J]] | |||
[[Category: Turner SJ]] | |||
Latest revision as of 13:19, 6 November 2024
Crystal Structure of 6218 TCR in complex with the H2Db-PA224Crystal Structure of 6218 TCR in complex with the H2Db-PA224
Structural highlights
FunctionB2MG_MOUSE Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMedPathogen-specific responses are characterized by preferred profiles of peptide+class I MHC (pMHCI) glycoprotein-specific T-cell receptor (TCR) Variable (V)-region use. How TCRV-region bias impacts TCRalphabeta heterodimer selection and resultant diversity is unclear. The D(b)PA(224)-specific TCR repertoire in influenza A virus-infected C57BL/6J (B6) mice exhibits a preferred TCRV-region bias toward the TRBV29 gene segment and an optimal complementarity determining region (CDR3) beta-length of 6 aa. Despite these restrictions, D(b)PA(224)-specific BV29(+) T cells use a wide array of unique CDR3beta sequences. Structural characterization of a single, TRBV29(+)D(b)P(A224)-specific TCRalphabeta-pMHCI complex demonstrated that CDR3alpha amino acid side chains made specific peptide interactions, but the CDR3beta main chain exclusively contacted peptides. Thus, length but not amino acid sequence was key for recognition and flexibility in Vbeta-region use. In support of this hypothesis, retrovirus expression of the D(b)PA(224)-specific TCRValpha-chain was used to constrain pairing within a naive/immune epitope-specific repertoire. The retrogenic TCRValpha paired with a diversity of CDR3betas in the context of a preferred TCRVbeta spectrum. Overall, these data provide an explanation for the combination of TCRV region bias and diversity within selected repertoires, even as they maintain exquisite pMHCI specificity. Structural basis for enabling T-cell receptor diversity within biased virus-specific CD8+ T-cell responses.,Day EB, Guillonneau C, Gras S, La Gruta NL, Vignali DA, Doherty PC, Purcell AW, Rossjohn J, Turner SJ Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9536-41. Epub 2011 May 23. PMID:21606376[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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