Structure and Function of Snake Venom Cardiotoxins
Cardiotoxins from elapid snake venoms are 'three-finger' shaped all β-sheet proteins with broad spectrum of biological properties. Members of this class possess strong membrane lytic property. Although, the amino acid sequences of cardiotoxins show more than 90% homology, the members of th...
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Published in: | Journal of toxicology. Toxin reviews Vol. 17; no. 2; pp. 183 - 211 |
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Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
Taylor & Francis
01-01-1998
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Subjects: | |
Online Access: | Get full text |
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Summary: | Cardiotoxins from elapid snake venoms are 'three-finger' shaped all β-sheet proteins with broad spectrum of biological properties. Members of this class possess strong membrane lytic property. Although, the amino acid sequences of cardiotoxins show more than 90% homology, the members of this class exhibit significant differences in erythrocyte lytic activity. Available evidence suggests that the 'active site' in cardiotoxins is constituted by non-polar and charged residues located in Loop 1 and Loop 2. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 |
ISSN: | 0731-3837 1525-6057 |
DOI: | 10.3109/15569549809009249 |