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Biochem Soc Trans. 2003 Aug;31(Pt 4):791-4.

Structure of human BPI (bactericidal/permeability-increasing protein) and implications for related proteins.

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  • 1Department of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, MO 65211, USA. beamerl@missouri.edu

Abstract

Human bactericidal/permeability-increasing protein (BPI) belongs to a family of mammalian lipopolysaccharide-binding and lipid transport proteins. Recent sequence database searches indicate that several other protein families, including the palate, lung and nasal epithelial clone (PLUNC), parotid secretory protein (PSP) and BPI-like proteins, are likely to share the BPI fold, which was determined through X-ray crystallographic studies. As the single representative of its fold family of known structure, the three-dimensional model of BPI suggests structural features that are likely to be conserved across this large and varied group of proteins.

PMID:
12887307
DOI:
10.1042/
[PubMed - indexed for MEDLINE]
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