2ak4: Difference between revisions

Revision as of 16:21, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ak4.png

Template:STRUCTURE 2ak4

Crystal Structure of SB27 TCR in complex with HLA-B3508-13mer peptideCrystal Structure of SB27 TCR in complex with HLA-B3508-13mer peptide

Template:ABSTRACT PUBMED 16186824

About this StructureAbout this Structure

2AK4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide., Tynan FE, Burrows SR, Buckle AM, Clements CS, Borg NA, Miles JJ, Beddoe T, Whisstock JC, Wilce MC, Silins SL, Burrows JM, Kjer-Nielsen L, Kostenko L, Purcell AW, McCluskey J, Rossjohn J, Nat Immunol. 2005 Nov;6(11):1114-22. Epub 2005 Sep 25. PMID:16186824

Page seeded by OCA on Sun Jul 27 16:21:43 2008

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OCA

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-'''Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide'''
+===Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide===
-==Overview==
+<!--
-Unusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction.
+The line below this paragraph, {{ABSTRACT_PUBMED_16186824}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16186824 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16186824}}
 ==About this Structure==
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 [[Category: Pmhc/tcr complex]]
 [[Category: T cell receptor]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:21:43 2008''