1bp1: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bp1 OCA], [http://www.ebi.ac.uk/pdbsum/1bp1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bp1 RCSB]</span> | |||
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[[Category: Carroll, S F.]] | [[Category: Carroll, S F.]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: antibiotic]] | [[Category: antibiotic]] | ||
[[Category: bactericidal]] | [[Category: bactericidal]] | ||
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[[Category: permeability-increasing]] | [[Category: permeability-increasing]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:05:27 2008'' | ||
Revision as of 16:05, 30 March 2008
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| 1bp1, resolution 2.40Å | |||||||||||||
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| Sites: | C and N | ||||||||||||
| Ligands: | PC1 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN
Overview
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.
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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