Initial structural analysis of an α4β4C-type lectin from the venom ofCrotalus durissus terrificus
| Autor: | S. P. Zela, A. C. O. Cintra, Raghuvir K. Arni, Leandra Watanabe, Lisandra M. Gava, Mário T. Murakami |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular biology Activator (genetics) Stereochemistry Crotalus Lectin Venom Convulxin General Medicine Crystallography X-Ray biology.organism_classification Protein Subunits Tetramer Structural Biology C-type lectin Crotalid Venoms Immunology biology.protein Animals Lectins C-Type South American rattlesnake Molecular replacement Disulfides Crystallization Protein Structure Quaternary |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 59:1813-1815 |
| ISSN: | 0907-4449 |
| Popis: | Convulxin, an alphabeta C-type lectin, is a potent platelet activator isolated from the venom of the South American rattlesnake Crotalus durissus terrificus. It is a 26.5 kDa alphabeta heterodimer consisting of two homologous disulfide-linked chains. The crystals belong to space group I4, with unit-cell parameters a = b = 131.61, c = 121.85 A, and diffraction data were collected to 2.7 A. The structure was solved by molecular replacement and the asymmetric unit contains two alphabeta heterodimers, each of which forms a disulfide-linked cyclic alpha(4)beta(4) tetramer in the unit cell. These alpha(4)beta(4) tetramers are stacked to form a large solvent channel. |
| Databáze: | OpenAIRE |
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