1UMR
Crystal structure of the platelet activator convulxin, a disulfide linked a4b4 cyclic tetramer from the venom of Crotalus durissus terrificus
Summary for 1UMR
Entry DOI | 10.2210/pdb1umr/pdb |
Related | 1C3A |
Descriptor | CONVULXIN ALPHA, CONVULXIN BETA (3 entities in total) |
Functional Keywords | lectin, c-type lectin, platelet, sugar-binding protein, activator, snake venom, 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 | 61413.12 |
Authors | Murakami, M.T.,Zela, S.P.,Gava, L.M.,Michelan-Duarte, S.,Cintra, A.C.O.,Arni, R.K. (deposition date: 2003-08-28, release date: 2003-11-21, Last modification date: 2024-10-16) |
Primary citation | Murakami, M.T.,Zela, S.P.,Gava, L.M.,Michelan-Duarte, S.,Cintra, A.C.O.,Arni, R.K. Crystal Structure of the Platelet Activator Convulxin, a Disulfide Linked A4B4 Cyclic Tetramer from the Venom of Crotalus Durissus Terrificus Biochem.Biophys.Res.Commun., 310:478-, 2003 Cited by PubMed Abstract: 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. PubMed: 14521935DOI: 10.1016/J.BBRC.2003.09.032 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
