2eyt

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[[Image:2eyt.gif|left|200px]]
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{{Structure
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{{STRUCTURE_2eyt| PDB=2eyt | SCENE= }}
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|RELATEDENTRY=[[2eyr|2EYR]], [[2eys|2EYS]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyt OCA], [http://www.ebi.ac.uk/pdbsum/2eyt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2eyt RCSB]</span>
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'''A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition'''
'''A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition'''
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[[Category: Borg, N A.]]
[[Category: Borg, N A.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: Kjer-Nielsen, L.]]
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[[Category: natural killer t cell receptor]]
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[[Category: Natural killer t cell receptor]]
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[[Category: nkt cell receptor]]
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[[Category: Nkt cell receptor]]
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[[Category: nkt15]]
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[[Category: Nkt15]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:15:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:55:32 2008''
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Revision as of 00:15, 4 May 2008

Template:STRUCTURE 2eyt

A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition


Overview

Little is known regarding the basis for selection of the semi-invariant alphabeta T cell receptor (TCR) expressed by natural killer T (NKT) cells or how this mediates recognition of CD1d-glycolipid complexes. We have determined the structures of two human NKT TCRs that differ in their CDR3beta composition and length. Both TCRs contain a conserved, positively charged pocket at the ligand interface that is lined by residues from the invariant TCR alpha- and semi-invariant beta-chains. The cavity is centrally located and ideally suited to interact with the exposed glycosyl head group of glycolipid antigens. Sequences common to mouse and human invariant NKT TCRs reveal a contiguous conserved "hot spot" that provides a basis for the reactivity of NKT cells across species. Structural and functional data suggest that the CDR3beta loop provides a plasticity mechanism that accommodates recognition of a variety of glycolipid antigens presented by CD1d. We propose a model of NKT TCR-CD1d-glycolipid interaction in which the invariant CDR3alpha loop is predicted to play a major role in determining the inherent bias toward CD1d. The findings define a structural basis for the selection of the semi-invariant alphabeta TCR and the unique antigen specificity of NKT cells.

About this Structure

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

Reference

A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition., Kjer-Nielsen L, Borg NA, Pellicci DG, Beddoe T, Kostenko L, Clements CS, Williamson NA, Smyth MJ, Besra GS, Reid HH, Bharadwaj M, Godfrey DI, Rossjohn J, McCluskey J, J Exp Med. 2006 Mar 20;203(3):661-73. Epub 2006 Feb 27. PMID:16505140 Page seeded by OCA on Sun May 4 03:15:53 2008

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