1UOS
The Crystal Structure of the Snake Venom Toxin Convulxin
Summary for 1UOS
| Entry DOI | 10.2210/pdb1uos/pdb |
| Related | 1UMR |
| Descriptor | CONVULXIN ALPHA, CONVULXIN BETA (3 entities in total) |
| Functional Keywords | sugar-binding protein, lectin, convulxin, c-type lectin, snake toxin, gpvi, structural proteomics in europe, spine, structural genomics, sugar binding protein |
| Biological source | CROTALUS DURISSUS TERRIFICUS (SOUTH AMERICAN RATTLESNAKE) More |
| Cellular location | Secreted: O93426 O93427 |
| Total number of polymer chains | 4 |
| Total formula weight | 61555.27 |
| Authors | Batuwangala, T.,Leduc, M.,Gibbins, J.M.,Bon, C.,Jones, E.Y. (deposition date: 2003-09-22, release date: 2003-10-14, Last modification date: 2024-11-20) |
| Primary citation | Batuwangala, T.,Leduc, M.,Gibbins, J.M.,Bon, C.,Jones, E.Y. Structure of the Snake-Venom Toxin Convulxin Acta Crystallogr.,Sect.D, 60:46-, 2004 Cited by PubMed Abstract: 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. PubMed: 14684891DOI: 10.1107/S0907444903021620 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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