1uos
From Proteopedia
|  (New page: 200px<br /><applet load="1uos" size="450" color="white" frame="true" align="right" spinBox="true"  caption="1uos, resolution 2.7Å" /> '''THE CRYSTAL STRUCTURE...) | |||
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| - | [[Image:1uos.gif|left|200px]]<br /><applet load="1uos" size=" | + | [[Image:1uos.gif|left|200px]]<br /><applet load="1uos" size="350" color="white" frame="true" align="right" spinBox="true"  | 
| caption="1uos, resolution 2.7Å" /> | caption="1uos, resolution 2.7Å" /> | ||
| '''THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN'''<br /> | '''THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN'''<br /> | ||
| ==Overview== | ==Overview== | ||
| - | Snake venoms contain a number of proteins that interact with components of | + | 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== | ||
| - | 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:// | + | 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.]] | ||
| - | [[Category: Gibbins, J | + | [[Category: Gibbins, J M.]] | 
| - | [[Category: Jones, E | + | [[Category: Jones, E Y.]] | 
| [[Category: Leduc, M.]] | [[Category: Leduc, M.]] | ||
| - | [[Category: SPINE, Structural | + | [[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]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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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