The structure of phosphatidylinositol transfer protein α reveals sites for phospholipid binding and membrane association with major implications for its function

Autor: van Tiel, Claudia M., Schouten, Arie, Snoek, Gerry T., Gros, Piet, Wirtz, Karel W.A.
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Zdroj: FEBS Letters; Oct2002, Vol. 531 Issue 1, p69, 5p
Abstrakt: 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. [Copyright &y& Elsevier]
Databáze: Complementary Index
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