1BP1

CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN

1BP1 の概要

• エントリーDOI: 10.2210/pdb1bp1/pdb
• 分子名称: BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• 機能のキーワード: bactericidal, permeability-increasing, lipid-binding, lipopolysaccharide-binding, antibiotic
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52283.98

構造登録者

Beamer, L.J.,Carroll, S.F.,Eisenberg, D. (登録日: 1997-04-08, 公開日: 1997-09-04, 最終更新日: 2024-11-06)

主引用文献

Beamer, L.J.,Carroll, S.F.,Eisenberg, D.
Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.
Science, 276:1861-1864, 1997

PubMed Abstract: Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.

PubMed: 9188532
DOI: 10.1126/science.276.5320.1861

実験手法

X-RAY DIFFRACTION (2.4 Å)