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1uos

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Revision as of 13:05, 1 January 2020

The Crystal Structure of the Snake Venom Toxin Convulxin

Structural highlights

1uos is a 4 chain structure with sequence from Crotalus durissus terrificus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1umr
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SLA_CRODU] Snake venom lectin that activates platelets by binding to the platelet collagen receptor glycoprotein VI (GP6) (PubMed:9153205). The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is upstream the cytoskeletal translocation of GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ)(PubMed:16102113).^[1] ^[2] [SLB_CRODU] Snake venom lectin that activates platelets by binding to the platelet collagen receptor glycoprotein VI (GP6) (PubMed:9153205). The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is upstream the cytoskeletal translocation of GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ)(PubMed:16102113).^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Polgar J, Clemetson JM, Kehrel BE, Wiedemann M, Magnenat EM, Wells TN, Clemetson KJ. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J Biol Chem. 1997 May 23;272(21):13576-83. PMID:9153205
↑ Lu Q, Clemetson JM, Clemetson KJ. Translocation of GPIb and Fc receptor gamma-chain to cytoskeleton in mucetin-activated platelets. J Thromb Haemost. 2005 Sep;3(9):2065-76. PMID:16102113 doi:http://dx.doi.org/10.1111/j.1538-7836.2005.01481.x
↑ Polgar J, Clemetson JM, Kehrel BE, Wiedemann M, Magnenat EM, Wells TN, Clemetson KJ. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J Biol Chem. 1997 May 23;272(21):13576-83. PMID:9153205
↑ Lu Q, Clemetson JM, Clemetson KJ. Translocation of GPIb and Fc receptor gamma-chain to cytoskeleton in mucetin-activated platelets. J Thromb Haemost. 2005 Sep;3(9):2065-76. PMID:16102113 doi:http://dx.doi.org/10.1111/j.1538-7836.2005.01481.x
↑ Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY. Structure of the snake-venom toxin convulxin. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uos"

@@ Line 1: / Line 1: @@
 ==The Crystal Structure of the Snake Venom Toxin Convulxin==
-<StructureSection load='1uos' size='340' side='right' caption='[[1uos]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='1uos' size='340' side='right'caption='[[1uos]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1uos]] is a 4 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UOS FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Crotalus durissus terrificus]]
+[[Category: Large Structures]]
 [[Category: Batuwangala, T]]
 [[Category: Bon, C]]

1uos

From Proteopedia

Revision as of 13:05, 1 January 2020

The Crystal Structure of the Snake Venom Toxin Convulxin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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