Molecular characteristics of phosphoinositide binding.
Phosphoinositides in general and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2) or PIP(2)) in particular have been recently found to function as important regulators of ion channels. Yet, while specific residues have been identified that affect channel-PIP(2) interactions, the precise binding site of PIP(2) has not been determined in any case. In addition to binding ion channels, however, phosphoinositides interact with a plethora of other proteins, and in a number of cases, the crystallographic structures of the complexes have been determined. Based on a database of 25 complexed crystallographic structures, we have addressed the molecular characteristics of phosphoinositide binding to proteins. Implications to phosphoinositide binding to ion channels are also discussed.
Rosenhouse-Dantsker
Avia
A
Department of Structural and Chemical Biology, Mount Sinai School of Medicine, New York, NY, 10029, USA. Avia.Rosenhouse-Dantsker@mssm.edu
Logothetis
Diomedes E
DE
D000818:Animals; D006801:Humans; D007473:Ion Channels / Q000502:physiology; D008958:Models, Molecular; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000737:chemistry / Q000378:metabolism; D010716:Phosphatidylinositols / Q000737:chemistry / Q000378:metabolism*
D007473:Ion Channels; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols