1uos

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(New page: 200px<br /><applet load="1uos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uos, resolution 2.7&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1uos.gif|left|200px]]<br /><applet load="1uos" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1uos, resolution 2.7&Aring;" />
caption="1uos, resolution 2.7&Aring;" />
'''THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN'''<br />
'''THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN'''<br />
==Overview==
==Overview==
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Snake venoms contain a number of proteins that interact with components of, the haemostatic system that promote or inhibit events leading to, blood-clot formation. The snake-venom protein convulxin (Cvx) binds, glycoprotein (GP) VI, the platelet receptor for collagen, and triggers, signal transduction. Here, the 2.7 A resolution crystal structure of Cvx, is presented. In common with other members of this snake-venom protein, family, Cvx is an alphabeta-heterodimer and conforms to the C-type, lectin-fold topology. Comparison with other family members allows a set of, Cvx residues that form a concave surface to be putatively implicated in, GPVI binding. Unlike other family members, with the exception of, flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric, structure is consistent with Cvx clustering GPVI molecules on the surface, of platelets and as a result promoting signal transduction activity. The, Cvx structure and the location of the putative binding sites suggest a, model for this multimeric signalling assembly.
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Snake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly.
==About this Structure==
==About this Structure==
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1UOS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UOS OCA].
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1UOS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOS OCA].
==Reference==
==Reference==
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[[Category: Batuwangala, T.]]
[[Category: Batuwangala, T.]]
[[Category: Bon, C.]]
[[Category: Bon, C.]]
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[[Category: Gibbins, J.M.]]
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[[Category: Gibbins, J M.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
[[Category: Leduc, M.]]
[[Category: Leduc, M.]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: c-type lectin]]
[[Category: c-type lectin]]
[[Category: convulxin]]
[[Category: convulxin]]
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:16:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:47 2008''

Revision as of 13:26, 21 February 2008


1uos, resolution 2.7Å

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THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN

Overview

Snake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly.

About this Structure

1UOS is a Protein complex structure of sequences from Crotalus durissus terrificus. Full crystallographic information is available from OCA.

Reference

Structure of the snake-venom toxin convulxin., Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891

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