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- W2034656116 endingPage "90" @default.
- W2034656116 startingPage "80" @default.
- W2034656116 abstract "Members of the inhibitor of apoptosis (IAP) family are characterised by the presence of at least one baculoviral IAP repeat (BIR) domain. However, during the course of evolution, other globular modules have been adopted to perform distinct functions. Consequently, the IAP family is now recognised as consisting of members that perform critical functions in different aspects of cellular regulation. In this review, the structural diversity present within the IAP protein family is presented. Known structures of individual domains are discussed and their properties are described in light of recent data. In particular the plasticity of BIR domains and their ability to accommodate different binding partners is highlighted, as well as the importance of communication between the domains in regulating the covalent attachment of ubiquitin." @default.
- W2034656116 created "2016-06-24" @default.
- W2034656116 creator A5001864928 @default.
- W2034656116 creator A5076901371 @default.
- W2034656116 date "2015-03-01" @default.
- W2034656116 modified "2023-10-17" @default.
- W2034656116 title "IAPs: Modular regulators of cell signalling" @default.
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