Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution.
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Umland TC, Swaminathan S, Singh G, Warty V, Furey W, Pletcher J, Sax M
Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution.
Nat Struct Biol. 1994 Aug;1(8):538-45.
- PubMed ID
- 7664082 [ View in PubMed]
- Abstract
The Clara cell phospholipid-binding protein, previously referred to as CC10, is a homodimeric protein of M(r) 15,800. It is secreted into the bronchioalveolar lining layer in mammalian lung. A combination of X-ray crystallography and chemical analysis was used to determine that phosphatidylcholine and phosphatidylinositol are bound to the protein as isolated from human lung lavage. We now report the crystal structure of the protein-phospholipid complex at 1.9 A resolution. The phospholipid is bound inside the protein's large hydrophobic cavity. A model is proposed for the manner in which a channel may open to provide access to the cavity, allowing the binding or potential release of phospholipid.