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| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1uos]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1UOS FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1uos]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1UOS FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1umr|1umr]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uos OCA], [https://pdbe.org/1uos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uos RCSB], [https://www.ebi.ac.uk/pdbsum/1uos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uos ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uos OCA], [https://pdbe.org/1uos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uos RCSB], [https://www.ebi.ac.uk/pdbsum/1uos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uos ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/SLA_CRODU 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).<ref>PMID:9153205</ref> <ref>PMID:16102113</ref> [[https://www.uniprot.org/uniprot/SLB_CRODU 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).<ref>PMID:9153205</ref> <ref>PMID:16102113</ref>
| + | [https://www.uniprot.org/uniprot/SLA_CRODU 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).<ref>PMID:9153205</ref> <ref>PMID:16102113</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| [[Category: Crotalus durissus terrificus]] | | [[Category: Crotalus durissus terrificus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Batuwangala, T]] | + | [[Category: Batuwangala T]] |
- | [[Category: Bon, C]] | + | [[Category: Bon C]] |
- | [[Category: Gibbins, J M]] | + | [[Category: Gibbins JM]] |
- | [[Category: Jones, E Y]] | + | [[Category: Jones EY]] |
- | [[Category: Leduc, M]] | + | [[Category: Leduc M]] |
- | [[Category: C-type lectin]]
| + | |
- | [[Category: Convulxin]]
| + | |
- | [[Category: Gpvi]]
| + | |
- | [[Category: Lectin]]
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- | [[Category: Snake toxin]]
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- | [[Category: Spine]]
| + | |
- | [[Category: Structural genomic]]
| + | |
- | [[Category: Structural proteomics in europe]]
| + | |
- | [[Category: Sugar binding protein]]
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- | [[Category: Sugar-binding protein]]
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| Structural highlights
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]
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[3]
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
- ↑ 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
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