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The structure of phosphatidylinositol transfer protein α reveals sites for phospholipid binding and membrane association with major implications for its function
Author(s) -
van Tiel Claudia M,
Schouten Arie,
Snoek Gerry T,
Gros Piet,
Wirtz Karel W.A
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03403-8
Subject(s) - phospholipid , phosphatidylinositol , pi , phospholipid transfer protein , chemistry , membrane , binding site , inositol , biophysics , protein–lipid interaction , biochemistry , membrane protein , biology , receptor , signal transduction , integral membrane protein
Elucidation of the three‐dimensional structure of phosphatidylinositol transfer protein α (PI‐TPα) void of phospholipid revealed a site of membrane association connected to a channel for phospholipid binding. Near the top of the channel specific binding sites for the phosphorylcholine and phosphorylinositol head groups were identified. The structure of this open form suggests a mechanism by which PI‐TPα preferentially binds PI from a membrane interface. Modeling predicts that upon association of PI‐TPα with the membrane the inositol moiety of bound PI is accessible from the medium. Upon release from the membrane PI‐TPα adopts a closed structure with the phospholipid bound fully encapsulated. This structure provides new insights as to how PI‐TPα may play a role in PI metabolism.