1bp1
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1bp1.gif|left|200px]]<br /><applet load="1bp1" size=" | + | [[Image:1bp1.gif|left|200px]]<br /><applet load="1bp1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bp1, resolution 2.40Å" /> | caption="1bp1, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1BP1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PC1 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http:// | + | 1BP1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PC1:'>PC1</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BP1 OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: permeability-increasing]] | [[Category: permeability-increasing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:33:34 2008'' |
Revision as of 07:33, 3 February 2008
|
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 with as ligand. Known structural/functional Sites: and . 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 Sun Feb 3 09:33:34 2008
