1bp1
From Proteopedia
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| - | [[Image:1bp1.gif|left|200px]] | + | [[Image:1bp1.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN''' | + | {{Structure |
| + | |PDB= 1bp1 |SIZE=350|CAPTION= <scene name='initialview01'>1bp1</scene>, resolution 2.40Å | ||
| + | |SITE= <scene name='pdbsite=C:Apolar+Pocket+Primarily+In+C-Terminal+Domain+Of+Protein+...'>C</scene> and <scene name='pdbsite=N:Apolar+Pocket+Primarily+In+N-Terminal+Domain+Of+Protein+...'>N</scene> | ||
| + | |LIGAND= <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BP1 is a [ | + | 1BP1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BP1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9188532 9188532] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: permeability-increasing]] | [[Category: permeability-increasing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:13:53 2008'' |
Revision as of 08:13, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Sites: | and | ||||||
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| 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
Page seeded by OCA on Thu Mar 20 10:13:53 2008
