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RESEARCH PRODUCT
Snake venom disintegrins: evolution of structure and function.
Cezary MarcinkiewiczVicent EsteveVicent EsteveDaniel MonleonJuan J. CalveteBernardo CeldaLibia SanzPaula Juárezsubject
Models MolecularIntegrinsStereochemistryDisintegrinsIntegrinAmino Acid MotifsMolecular Sequence DataSequence alignmentVenomToxicologyViper VenomsEvolution MolecularStructure-Activity RelationshipProtein structureGenes DuplicateAnimalsAmino Acid SequencePeptide sequencePhylogenybiologyBase SequenceSnakesCell biologyProtein Structure TertiarySnake venombiology.proteinSequence AlignmentFunction (biology)Snake Venomsdescription
Disintegrins represent a family of polypeptides present in the venoms of various vipers that selectively block the function of integrin receptors. Here, we review our current view and hypothesis on the emergence and the structural and functional diversification of disintegrins by accelerated evolution and the selective loss of disulfide bonds of duplicated genes. Research on disintegrins is relevant for understanding the biology of viper venom toxins, but also provides information on new structural determinants involved in integrin recognition that may be useful in basic and clinical research. The role of the composition, conformation, and dynamics of the integrin inhibitory loop acting in concert with the C-terminal tail in determining the selective inhibition of integrin receptors is discussed.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2005-02-23 | Toxicon : official journal of the International Society on Toxinology |