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1lk2
From Proteopedia
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(New page: 200px<br /><applet load="1lk2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lk2, resolution 1.35Å" /> '''1.35A crystal struct...)
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Revision as of 18:29, 20 November 2007
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1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide
Overview
We identify and consider some characteristics of a peptide antagonist for, the Ag-specific receptor on 2C cells (the 2C TCR). The peptide, GNYSFYAL, (called GNY), binds to H-2K(b), and a very high-resolution crystal, structure of the GNY-K(b) complex at 1.35 A is described. Although the GNY, peptide does not bind to L(d), the potency of GNY-K(b) as an antagonist is, evident from its ability to specifically inhibit 2C TCR-mediated reactions, to an allogenic agonist complex (QLSPFPFDL-L(d)), as well as to a, syngeneic agonist complex (SIYRYYGL-K(b)). The crystal structure and the, activities of alanine-substituted peptide variants point to the properties, of the peptide P4 side chain and the conformation of the Tyr-P6 side chain, as the structural determinants of GNYSFYAL antagonist activity.
About this Structure
1LK2 is a Protein complex structure of sequences from Mus musculus with NAG, PO4, MRD and MPD as ligands. Full crystallographic information is available from OCA.
Reference
A peptide that antagonizes TCR-mediated reactions with both syngeneic and allogeneic agonists: functional and structural aspects., Rudolph MG, Shen LQ, Lamontagne SA, Luz JG, Delaney JR, Ge Q, Cho BK, Palliser D, McKinley CA, Chen J, Wilson IA, Eisen HN, J Immunol. 2004 Mar 1;172(5):2994-3002. PMID:14978103
Page seeded by OCA on Tue Nov 20 20:36:58 2007
