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Sci. STKE, 29 August 2000
Vol. 2000, Issue 47, p. tw12
[DOI: 10.1126/stke.2000.47.tw12]

EDITORS' CHOICE

Review Lipid Binding Domains

Signals can be regulated by many flexible strategies, including blocking protein catalytic activity, reducing product accumulation, or sequestrating proteins from their site of action. Several protein binding domains that regulate the interaction of proteins with each other have been identified. More recently, the binding domains that allow proteins to bind lipids and, therefore, the plasma membrane have gained increased appreciation. Hurley and Misra review the domains that specifically bind lipid moities. Of great importance is understanding the subtle differences in overall domain structures and how these differences relate to binding specificity. For example, within the C2 domain family, some members bind lipids or proteins and do so in the presence or absence of Ca2+. Of course, as the authors point out, specificity is imparted by the residues flanking each domain and by less conserved residues within the domain. The moderately biophysical approach taken by Hurley and Misra provides a fresh view on a subject often covered.

Hurley, J.H., and Misra, S. (2000) Signaling and subcellular targeting by membrane-binding domains. Annu. Rev. Biophys. Biomol. Struct. 29: 49-79. [Abstract] [Full Text]

Citation: Lipid Binding Domains. Sci. STKE 2000, tw12 (2000).


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