1LN2

Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine (Seleno-Met Protein)

1LN2 の概要

• エントリーDOI: 10.2210/pdb1ln2/pdb
• 関連するPDBエントリー: 1LN1 1LN3
• 分子名称: Phosphatidylcholine transfer protein, 1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• 機能のキーワード: start domain, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q9UKL6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51963.29

構造登録者

Roderick, S.L.,Chan, W.W.,Agate, D.S.,Olsen, L.R.,Vetting, M.W.,Rajashankar, K.R.,Cohen, D.E. (登録日: 2002-05-02, 公開日: 2002-06-26, 最終更新日: 2024-10-09)

主引用文献

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

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: 12055623

実験手法

X-RAY DIFFRACTION (2.9 Å)