Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 DOI10.2210/pdb1umr/pdb
Related1C3A
DescriptorCONVULXIN ALPHA, CONVULXIN BETA (3 entities in total)
Functional Keywordslectin, c-type lectin, platelet, sugar-binding protein, activator, snake venom, sugar binding protein
Biological sourceCROTALUS DURISSUS TERRIFICUS (SOUTH AMERICAN RATTLESNAKE)
More
Cellular locationSecreted: O93426 O93427
Total number of polymer chains4
Total formula weight61413.12
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 citationMurakami, 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: 14521935
DOI: 10.1016/J.BBRC.2003.09.032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon