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• W2584667069 abstract "A wide range of lipid second messengers that are generated in response to external signals has been characterized in terms of their molecular biology. This review will focus on underlying structural principles involved in recognizing these messengers both by the enzymes that produce or consume them and by the downstream effector domains. In most cases, the lipid-modifying enzymes are structurally homologous to enzymes that catalyze an analogous reaction using soluble substrates, suggesting that the constraintsimposed by the catalytic chemistry are a stronger determinant of fold than specific lipid binding. Although much progress has been made in defining the nature of the interactions of lipid second messengers with proteins, many questions remain unanswered. several lipid second messengers have been characterized for which there is no structural information about specific binding modules, e.g. PtdIns(3,5)P 2 and phosphatidic acid. A dimension of response to lipid-messenger recognition that remains largely unexplored is the effect of membrane binding on membrane structure during processes such as formation of multivesicular bodies. Many proteins use multiple weak interactions to bind to membranes in response to lipid second messengers, but an analysis of the energetics of the individual interactions is often lacking. Although membrane translocation in response to lipid second messengers is common, the nature and extent of allosteric responses mediated by membrane interactions are not clear. With methodologies thathave emerged in the wake of genomic studies, one can look forward to answers to many of these questions in the near future." @default.
• W2584667069 created "2017-02-10" @default.
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• W2584667069 date "2003-01-01" @default.
• W2584667069 modified "2023-09-27" @default.
• W2584667069 title "Structural Principles of Lipid Second Messenger Recognition" @default.
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• W2584667069 doi "https://doi.org/10.1016/b978-012124546-7/50510-6" @default.
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