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. Author manuscript; available in PMC: 2009 Sep 14.
Published in final edited form as: Biochim Biophys Acta. 2007 Apr 12;1771(6):654–662. doi: 10.1016/j.bbalip.2007.04.003

Figure 1.

Figure 1

A) Overall structure of human PC-TP. The α-helix identifiers and residue ranges for human PC-TP are α1 (9–22), α2 (64–74), α3 (75–82) and α4 (184–209). The β-strand identifiers and residue ranges are β1 (31–36), β2 (39–46), β3 (51–61), β4 (84–93), β5 (96–104), β6 (111–123), β7 (130–138), β8 (150–162) and β9 (168–178). The Ω-loop identifiers and residue ranges are Ω1 (105–110) and Ω2 (139–149). B) Interactions of PC-TP (blue) with the glycerol-3-phosphorylcholine moiety of 1-palmitoyl,2-linoleoyl-sn-glycerol-3-phosphorylcholine (palmitoyl-linoleoyl phosphatidylcholine) (yellow). The structure of 1,2-dilinoleoyl-sn-glycerol-3-phosphorylcholine (dilinoleoyl phosphatidylcholine) from the PC-TP–phosphatidylcholine complex is superimposed (gray). C) Solvent accessible volume of the binding pocket containing phosphatidylcholine. The phosphatidylcholine molecule occupies approximately 89% of the lipid binding pocket, which extends through two narrow portals 3–5 Å in diameter to bulk solvent. (Reprinted with permission from reference [26]).