Molecular diversity of disintegrin-like domains within metalloproteinase precursors of Bothrops jararaca
| Autor: | Alberto M. R. Dávila, Luciana S. Wermelinger, Rodolpho Mattos Albano, Gisele Lôbo-Hajdu, Daniela Anhel de Paula Cidade, Russolina B. Zingali, Cassian Bon |
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| Rok vydání: | 2006 |
| Předmět: |
DNA
Complementary Bothrops jararaca Sequence analysis Disintegrins Molecular Sequence Data Venom Matrix metalloproteinase Toxicology Structure-Activity Relationship Species Specificity Catalytic Domain Crotalid Venoms Disintegrin Animals Bothrops Amino Acid Sequence Phylogeny Enzyme Precursors Metalloproteinase biology cDNA library Genetic Variation biology.organism_classification Biochemistry Snake venom Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Metalloproteases biology.protein Sequence Alignment |
| Zdroj: | Toxicon. 48:590-599 |
| ISSN: | 0041-0101 |
| Popis: | Disintegrins are small peptides isolated from the venom of several snake families which act as integrin-antagonists or agonists, interacting with a variety of biological processes mediated by integrins. In this work we describe five new disintegrin-like domains within metalloproteinase precursor sequences, obtained from a Bothrops jararaca venom gland cDNA library. Among the new disintegrin-like domains, four were contained in PIII metalloproteinase precursors, with three of them presenting ECD-motifs and one presenting a new KCD-motif. Moreover, we found three disintegrin-like domains within PII metalloproteinase precursors. Two of them are similar to the already described disintegrins jarastatin and jararacin. The third molecule is unusual, presenting some typical PIII metalloproteinase characteristics but lacking the cysteine-rich domain being, thus, classified as a PII metalloproteinase. Only few reports presented molecules with these characteristics. Sequence analysis suggests that these molecules are intermediate steps between the more ancient PIII and the more recent PII metalloproteinases. We also investigated disintegrin N-terminus diversity in B. jararaca crude venom by purifying jarastatin and jararacin and analyzing them by mass spectrometry. |
| Databáze: | OpenAIRE |
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