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

被引:39
作者
Beamer, LJ [1 ]
机构
[1] Univ Missouri, Dept Biochem, Columbia, MO 65211 USA
关键词
BPI; homology modelling; X-ray crystallography;
D O I
10.1042/bst0310791
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:791 / 794
页数:4
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