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1z5l

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(New page: 200px<br /><applet load="1z5l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5l, resolution 2.20&Aring;" /> '''Structure of a highl...)
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Revision as of 05:07, 21 November 2007

Image:1z5l.gif

1z5l, resolution 2.20Å

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Structure of a highly potent short-chain galactosyl ceramide agonist bound to CD1D

Overview

Natural killer T cells express a conserved, semi-invariant alphabeta T, cell receptor that has specificity for self glycosphingolipids and, microbial cell wall alpha-glycuronosylceramide antigens presented by CD1d, molecules. Here we report the crystal structure of CD1d in complex with a, short-chain synthetic variant of alpha-galactosylceramide at a resolution, of 2.2 A. This structure elucidates the basis for the high specificity of, these microbial ligands and explains the restriction of the alpha-linkage, as a unique pathogen-specific pattern-recognition motif. Comparison of the, binding of altered lipid ligands to CD1d and T cell receptors suggested, that the differential T helper type 1-like and T helper type 2-like, properties of natural killer T cells may originate largely from, differences in their 'loading' in different cell types and hence in their, tissue distribution in vivo.

About this Structure

1Z5L is a Protein complex structure of sequences from Mus musculus with NAG, PBS and R16 as ligands. Full crystallographic information is available from OCA.

Reference

Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor., Zajonc DM, Cantu C 3rd, Mattner J, Zhou D, Savage PB, Bendelac A, Wilson IA, Teyton L, Nat Immunol. 2005 Aug;6(8):810-8. Epub 2005 Jul 10. PMID:16007091

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