1llr

From Proteopedia
Revision as of 03:58, 25 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1llr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llr, resolution 1.460Å" /> '''CHOLERA TOXIN B-PEN...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1llr.jpg


1llr, resolution 1.460Å

Drag the structure with the mouse to rotate

CHOLERA TOXIN B-PENTAMER WITH LIGAND BMSC-0012

OverviewOverview

Multivalent ligand design constitutes an attractive avenue to the, inhibition of receptor recognition and other biological events mediated by, oligomeric proteins with multiple binding sites. One example is the design, of multivalent receptor blockers targeting members of the AB(5) bacterial, toxin family. We report here the synthesis and characterization of a, pentavalent inhibitor for cholera toxin and Escherichia coli heat-labile, enterotoxin. This inhibitor is an advance over the symmetric, pentacyclen-derived inhibitor described in our earlier work in that it, presents five copies of m-nitrophenyl-alpha-D-galactoside (MNPG) rather, than five copies of beta-D-galactose. The approximately 100-fold higher, single-site affinity of MNPG for the toxin receptor binding site relative, to galactose is found to yield a proportionate increase in the affinity, and IC50 measured for the respective pentavalent constructs. We show by, dynamic light scattering that inhibition of receptor binding by the, pentavalent inhibitor is due to 1:1 inhibitor:toxin association rather, than to inhibitor-mediated aggregation. This 1:1 association is in, complete agreement with a 1.46 A resolution crystal structure of the, pentavalent inhibitor:toxin complex, which shows that the favorable, single-site binding interactions of MNPG are retained by the five arms of, the 5256 Da pentavalent MNPG-based inhibitor and that the initial segment, of the linking groups interacts with the surface of the toxin B pentamer.

About this StructureAbout this Structure

1LLR is a Single protein structure of sequence from Vibrio cholerae with FNG as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Characterization and crystal structure of a high-affinity pentavalent receptor-binding inhibitor for cholera toxin and E. coli heat-labile enterotoxin., Merritt EA, Zhang Z, Pickens JC, Ahn M, Hol WG, Fan E, J Am Chem Soc. 2002 Jul 31;124(30):8818-24. PMID:12137534

Page seeded by OCA on Sun Nov 25 03:06:30 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA