1bxp

From Proteopedia
Revision as of 12:53, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1bxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxp" /> '''SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALP...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1bxp.gif


1bxp

Drag the structure with the mouse to rotate

SOLUTION NMR STRUCTURE OF THE COMPLEX OF ALPHA-BUNGAROTOXIN WITH A LIBRARY DERIVED PEPTIDE, 20 STRUCTURES

OverviewOverview

The solution structure of the complex between alpha-bungarotoxin, (alpha-BTX) and a 13-residue library-derived peptide (MRYYESSLKSYPD) has, been solved using two-dimensional proton-NMR spectroscopy. The bound, peptide adopts an almost-globular conformation resulting from three turns, that surround a hydrophobic core formed by Tyr-11 of the peptide. The, peptide fills an alpha-BTX pocket made of residues located at fingers I, and II, as well as at the C-terminal region. Of the peptide residues, the, largest contact area is formed by Tyr-3 and Tyr-4. These findings are in, accord with the previous data in which it had been shown that substitution, of these aromatic residues by aliphatic amino acids leads to loss of, binding of the modified peptide with alpha-BTX. Glu-5 and Leu-8, which, also remarkably contribute to the contact area with the toxin, are present, in all the library-derived peptides that bind strongly to alpha-BTX. The, structure of the complex may explain the fact that the library-derived, peptide binds alpha-BTX with a 15-fold higher affinity than that shown by, the acetylcholine receptor peptide (alpha185-196). Although both peptides, bind to similar sites on alpha-BTX, the latter adopts an extended, conformation when bound to the toxin [Basus, V., Song, G. & Hawrot, E., (1993) Biochemistry 32, 12290-12298], whereas the library peptide is, nearly globular and occupies a larger surface area of alpha-BTX binding, site.

About this StructureAbout this Structure

1BXP is a Single protein structure of sequence from Bungarus multicinctus. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptide., Scherf T, Balass M, Fuchs S, Katchalski-Katzir E, Anglister J, Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6059-64. PMID:9177168

Page seeded by OCA on Tue Nov 20 12:00:19 2007

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

OCA