Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.toxicon.2003.11.002
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dc.titleExcitement ahead: Structure, function and mechanism of snake venom phospholipase A2 enzymes
dc.contributor.authorKini, R.M.
dc.date.accessioned2014-10-27T08:48:17Z
dc.date.available2014-10-27T08:48:17Z
dc.date.issued2003-12
dc.identifier.citationKini, R.M. (2003-12). Excitement ahead: Structure, function and mechanism of snake venom phospholipase A2 enzymes. Toxicon 42 (8) : 827-840. ScholarBank@NUS Repository. <a href="https://doi.org/10.1016/j.toxicon.2003.11.002" target="_blank">https://doi.org/10.1016/j.toxicon.2003.11.002</a>
dc.identifier.issn00410101
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/102448
dc.description.abstractVenom phospholipase A2 (PLA2) enzymes share similarity in structure and catalytic function with mammalian enzymes. However, in contrast to mammalian enzymes, many are toxic and induce a wide spectrum of pharmacological effects. Thus structure-function relationship of this group of small proteins is subtle, but complex puzzle to protein biochemists, molecular biologists, toxinologists, pharmacologists and physiologists. This review describes the present status of our understanding of their structure, function and mechanism. It was proposed that their unique ability to 'target' themselves to a specific organ or tissue is due to their high affinity binding to specific proteins which act as receptors (more precisely, acceptors). This specific binding of PLA2 is conferred by the presence of a 'pharmacological site' on its surface which is independent of the catalytic site. The high affinity interaction of PLA2 with its acceptor (or target protein) is probably due to the complementarity, in terms of charges, hydrophobicity and van der Waal's contact surfaces, between the pharmacological site and the binding site on the surface of the acceptor protein. Upon binding to the target, the PLA2 can induce its pharmacological effects by mechanisms either dependent on or independent of its catalytic activity. Because of the unprecedented wide spectrum of specific targeting to various tissues and organs, identification of the pharmacological sites has potential for exploitation in development of novel systems useful for 'delivering' specific proteins to a particular target tissue or organ. Thus research in this field will provide a lot of exciting opportunities. © 2003 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.toxicon.2003.11.002
dc.sourceScopus
dc.subjectAcceptor
dc.subjectAnticoagulant
dc.subjectMyotoxin
dc.subjectNeurotoxin
dc.subjectProtein-protein interaction
dc.subjectSnake venom
dc.subjectToxin receptor
dc.typeReview
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.toxicon.2003.11.002
dc.description.sourcetitleToxicon
dc.description.volume42
dc.description.issue8
dc.description.page827-840
dc.description.codenTOXIA
dc.identifier.isiutNOT_IN_WOS
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