Structure of human BPI (bactericidal/permeability-increasing protein) and implications for related proteins.
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.
Beamer
L J
LJ
Department of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, MO 65211, USA. beamerl@missouri.edu
D000209:Acute-Phase Proteins; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins / Q000737:chemistry* / Q000235:genetics; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics; D006801:Humans; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D000099231:Lipopolysaccharide-Binding Protein
D000209:Acute-Phase Proteins; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D000099231:Lipopolysaccharide-Binding Protein; C021623:bactericidal permeability increasing protein; C030363:lipid transfer protein