期刊
FEBS LETTERS
卷 531, 期 1, 页码 69-73出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03403-8
关键词
phosphatidylinositol; phosphatidylcholine; lipid-binding site; open and closed conformation
Elucidation of the three-dimensional structure of phosphatidylinositol transfer protein alpha (PI-TPalpha) 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-TPalpha preferentially binds PI from a membrane interface. Modeling predicts that upon association of PI-TPalpha with the membrane the inositol moiety of bound PI is accessible from the medium. Upon release from the membrane PI-TPalpha adopts a closed structure with the phospholipid bound fully encapsulated. This structure provides new insights as to how PI-TPalpha may play a role in PI metabolism. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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