Structure of a human clara cell dhospholipid-binding protein- igand complex at 1.9 å resolution

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

Research output: Contribution to journalArticle

73 Citations (Scopus)

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 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.

Original languageEnglish (US)
Pages (from-to)538-545
Number of pages8
JournalNature Structural Biology
Volume1
Issue number8
DOIs
StatePublished - Jan 1 1994
Externally publishedYes

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Phospholipids
Carrier Proteins
Proteins
X ray crystallography
X Ray Crystallography
Bronchoalveolar Lavage
Phosphatidylcholines
Linings
Crystal structure
Lung
Chemical analysis

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

Cite this

Structure of a human clara cell dhospholipid-binding protein- igand complex at 1.9 å resolution. / Umland, Timothy C.; Swaminathan, S.; Singh, Gurmukh; Warty, Vijay; Furey, William; Pletcher, James; Sax, Martin.

In: Nature Structural Biology, Vol. 1, No. 8, 01.01.1994, p. 538-545.

Research output: Contribution to journalArticle

Umland, Timothy C. ; Swaminathan, S. ; Singh, Gurmukh ; Warty, Vijay ; Furey, William ; Pletcher, James ; Sax, Martin. / Structure of a human clara cell dhospholipid-binding protein- igand complex at 1.9 å resolution. In: Nature Structural Biology. 1994 ; Vol. 1, No. 8. pp. 538-545.
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