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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[1umr]] 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=1UMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMR FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1umr]] 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=1UMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMR 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;'>[[1c3a|1c3a]]</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]] 2.4Å</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=1umr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umr OCA], [https://pdbe.org/1umr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umr RCSB], [https://www.ebi.ac.uk/pdbsum/1umr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umr 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=1umr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umr OCA], [https://pdbe.org/1umr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umr RCSB], [https://www.ebi.ac.uk/pdbsum/1umr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umr 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: Arni, R K]] | + | [[Category: Arni RK]] |
| - | [[Category: Cintra, A C.O]] | + | [[Category: Cintra ACO]] |
| - | [[Category: Gava, L M]] | + | [[Category: Gava LM]] |
| - | [[Category: Michelan-Duarte, S]] | + | [[Category: Michelan-Duarte S]] |
| - | [[Category: Murakami, M T]] | + | [[Category: Murakami MT]] |
| - | [[Category: Zela, S P]] | + | [[Category: Zela SP]] |
| - | [[Category: Activator]]
| + | |
| - | [[Category: C-type lectin]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Platelet]]
| + | |
| - | [[Category: Snake venom]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Sugar-binding protein]]
| + | |
| 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
Convulxin (CVX), a C-type lectin, isolated from the venom of the South American rattlesnake Crotalus durissus terrificus, causes cardiovascular and respiratory disturbances and is a potent platelet activator which binds to platelet glycoprotein GPVI. The structure of CVX has been solved at 2.4A resolution to a crystallographic residual of 18.6% (R(free)=26.4%). CVX is a disulfide linked heterodimer consisting of homologous alpha and beta chains. The heterodimers are additionally linked by disulfide bridges to form cyclic alpha(4)beta(4)heterotetramers. These domains exhibit significant homology to the carbohydrate-binding domains of C-type lectins, to the factor IX-binding protein (IX-bp), and to flavocetin-A (Fl-A) but sequence and structural differences are observed in both the domains in the putative Ca(2+)and carbohydrate binding regions.
Crystal structure of the platelet activator convulxin, a disulfide-linked alpha4beta4 cyclic tetramer from the venom of Crotalus durissus terrificus.,Murakami MT, Zela SP, Gava LM, Michelan-Duarte S, Cintra AC, Arni RK Biochem Biophys Res Commun. 2003 Oct 17;310(2):478-82. PMID:14521935[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
- ↑ Murakami MT, Zela SP, Gava LM, Michelan-Duarte S, Cintra AC, Arni RK. Crystal structure of the platelet activator convulxin, a disulfide-linked alpha4beta4 cyclic tetramer from the venom of Crotalus durissus terrificus. Biochem Biophys Res Commun. 2003 Oct 17;310(2):478-82. PMID:14521935
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