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Structure of a human Clara cell phospholipid-binding protein–ligand complex at 1. 9 Å resolution

Nature Structural Biology volume 1, pages 538–545 (1994)Cite this article

Abstract

The Clara cell phospholipid-binding protein, previously referred to as CC10, is a homodimeric protein of Mr 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 phophatidylinositol 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 Å 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.

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Authors and Affiliations

  1. VA Medical Center, P. O. Box 12055, University Drive C, Pittsburgh, Pennsylvania, 15240, USA

    Timothy C. Umland, S. Swaminathan, Gurmukh Singh, Vijay Warty, William Furey, James Pletcher & Martin Sax

  2. Department of Crystallography, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    Timothy C. Umland, S. Swaminathan, William Furey, James Pletcher & Martin Sax

  3. Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, 15260, USA

    Gurmukh Singh & Vijay Warty

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  1. Timothy C. Umland
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  2. S. Swaminathan
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Umland, T., Swaminathan, S., Singh, G. et al. Structure of a human Clara cell phospholipid-binding protein–ligand complex at 1. 9 Å resolution. Nat Struct Mol Biol 1, 538–545 (1994). https://doi.org/10.1038/nsb0894-538

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