1LN1
Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine
Summary for 1LN1
Entry DOI | 10.2210/pdb1ln1/pdb |
Related | 1LN2 1LN3 |
Descriptor | Phosphatidylcholine transfer protein, 1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total) |
Functional Keywords | start domain, lipid binding protein |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm : Q9UKL6 |
Total number of polymer chains | 1 |
Total formula weight | 25653.38 |
Authors | Roderick, S.L.,Chan, W.W.,Agate, D.S.,Olsen, L.R.,Vetting, M.W.,Rajashankar, K.R.,Cohen, D.E. (deposition date: 2002-05-02, release date: 2002-06-26, Last modification date: 2024-11-20) |
Primary citation | Roderick, S.L.,Chan, W.W.,Agate, D.S.,Olsen, L.R.,Vetting, M.W.,Rajashankar, K.R.,Cohen, D.E. Structure of human phosphatidylcholine transfer protein in complex with its ligand. Nat.Struct.Biol., 9:507-511, 2002 Cited by PubMed Abstract: 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. PubMed: 12055623PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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