1ln1
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Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine
OverviewOverview
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.
About this StructureAbout this Structure
1LN1 is a Single protein structure of sequence from Homo sapiens with DLP as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human phosphatidylcholine transfer protein in complex with its ligand., Roderick SL, Chan WW, Agate DS, Olsen LR, Vetting MW, Rajashankar KR, Cohen DE, Nat Struct Biol. 2002 Jul;9(7):507-11. PMID:12055623
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