1uos
From Proteopedia
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| - | [[Image:1uos.gif|left|200px]] | + | [[Image:1uos.gif|left|200px]] | 
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| - | '''THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN''' | + |  {{Structure | 
| + | |PDB= 1uos |SIZE=350|CAPTION= <scene name='initialview01'>1uos</scene>, resolution 2.7Å | ||
| + | |SITE=  | ||
| + | |LIGAND=  | ||
| + | |ACTIVITY=  | ||
| + | |GENE=  | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN''' | ||
| + | |||
| ==Overview== | ==Overview== | ||
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| ==About this Structure== | ==About this Structure== | ||
| - | 1UOS is a [ | + | 1UOS is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14684891 14684891] | 
| [[Category: Crotalus durissus terrificus]] | [[Category: Crotalus durissus terrificus]] | ||
| [[Category: Protein complex]] | [[Category: Protein complex]] | ||
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| [[Category: snake toxin]] | [[Category: snake toxin]] | ||
| [[Category: spine]] | [[Category: spine]] | ||
| - | [[Category: structural  | + | [[Category: structural genomic]] | 
| [[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:34:52 2008'' | 
Revision as of 12:34, 20 March 2008
 
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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