1lk2

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(New page: 200px<br /><applet load="1lk2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lk2, resolution 1.35&Aring;" /> '''1.35A crystal struct...)
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[[Image:1lk2.gif|left|200px]]<br /><applet load="1lk2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lk2.gif|left|200px]]<br /><applet load="1lk2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lk2, resolution 1.35&Aring;" />
caption="1lk2, resolution 1.35&Aring;" />
'''1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide'''<br />
'''1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1LK2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG, PO4, MRD and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LK2 OCA].
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1LK2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MRD:'>MRD</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK2 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Eisen, H.]]
[[Category: Eisen, H.]]
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[[Category: Luz, J.G.]]
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[[Category: Luz, J G.]]
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[[Category: Rudolph, M.G.]]
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[[Category: Rudolph, M G.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: MPD]]
[[Category: MPD]]
[[Category: MRD]]
[[Category: MRD]]
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[[Category: high resolution]]
[[Category: high resolution]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:36:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:41 2008''

Revision as of 11:45, 21 February 2008


1lk2, resolution 1.35Å

Drag the structure with the mouse to rotate

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 , , and 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

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