1bp1

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[[Image:1bp1.gif|left|200px]]
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{{STRUCTURE_1bp1| PDB=1bp1 | SCENE= }}
{{STRUCTURE_1bp1| PDB=1bp1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN'''
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===CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9188532 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9188532}}
==About this Structure==
==About this Structure==
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[[Category: Lipopolysaccharide-binding]]
[[Category: Lipopolysaccharide-binding]]
[[Category: Permeability-increasing]]
[[Category: Permeability-increasing]]
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Revision as of 16:29, 30 June 2008

Image:1bp1.png

Template:STRUCTURE 1bp1

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

Template:ABSTRACT PUBMED 9188532

About this Structure

1BP1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution., Beamer LJ, Carroll SF, Eisenberg D, Science. 1997 Jun 20;276(5320):1861-4. PMID:9188532

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