1ln3: Difference between revisions

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[[Image:1ln3.jpg|left|200px]]
{{Seed}}
[[Image:1ln3.png|left|200px]]


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{{STRUCTURE_1ln3|  PDB=1ln3  |  SCENE=  }}  
{{STRUCTURE_1ln3|  PDB=1ln3  |  SCENE=  }}  


'''Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein)'''
===Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein)===




==Overview==
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Phosphatidylcholines (PtdChos) comprise the most common phospholipid class in eukaryotic cells. In mammalian cells, these insoluble molecules are transferred between membranes by a highly specific phosphatidylcholine transfer protein (PC-TP) belonging to the steroidogenic acute regulatory protein related transfer (START) domain superfamily of hydrophobic ligand-binding proteins. The crystal structures of human PC-TP in complex with dilinoleoyl-PtdCho or palmitoyl-linoleoyl-PtdCho reveal that a single well-ordered PtdCho molecule occupies a centrally located tunnel. The positively charged choline headgroup of the lipid engages in cation-pi interactions within a cage formed by the faces of three aromatic residues. These binding determinants and those for the phosphoryl group may be exposed to the lipid headgroup at the membrane-water interface by a conformational change involving the amphipathic C-terminal helix and an Omega-loop. The structures presented here provide a basis for rationalizing the specificity of PC-TP for PtdCho and may identify common features used by START proteins to bind their hydrophobic ligands.
The line below this paragraph, {{ABSTRACT_PUBMED_12055623}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12055623}}


==About this Structure==
==About this Structure==
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[[Category: Vetting, M W.]]
[[Category: Vetting, M W.]]
[[Category: Start domain]]
[[Category: Start domain]]
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