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1haa

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{{STRUCTURE_1haa| PDB=1haa | SCENE= }}
{{STRUCTURE_1haa| PDB=1haa | SCENE= }}
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'''A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT BINDS A-BUNGAROTOXIN WITH HIGH AFFINITY AND NEUTRALIZES ITS TOXICITY'''
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===A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT BINDS A-BUNGAROTOXIN WITH HIGH AFFINITY AND NEUTRALIZES ITS TOXICITY===
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==Overview==
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Snake-venom alpha-bungarotoxin is a member of the alpha-neurotoxin family that binds with very high affinity to the nicotinic acetylcholine receptor (AChR) at the neuromuscular junction. The structure of the complex between alpha-bungarotoxin and a 13-mer peptide (WRYYESSLEPYPD) that binds the toxin with high affinity, thus inhibiting its interactions with AChR with an IC(50) of 2 nM, has been solved by (1)H-NMR spectroscopy. The bound peptide folds into a beta-hairpin structure created by two antiparallel beta-strands, which combine with the already existing triple-stranded beta-sheet of the toxin to form a five-stranded intermolecular, antiparallel beta-sheet. Peptide residues Y3(P), E5(P), and L8(P) have the highest intermolecular contact area, indicating their importance in the binding of alpha-bungarotoxin; W1(P), R2(P), and Y4(P) also contribute significantly to the binding. A large number of characteristic hydrogen bonds and electrostatic and hydrophobic interactions are observed in the complex. The high-affinity peptide exhibits inhibitory potency that is better than any known peptide derived from AChR, and is equal to that of the whole alpha-subunit of AChR. The high degree of sequence similarity between the peptide and various types of AChRs implies that the binding mode found within the complex might possibly mimic the receptor binding to the toxin. The design of the high-affinity peptide was based on our previous findings: (i) the detection of a lead peptide (MRYYESSLKSYPD) that binds alpha-bungarotoxin, using a phage-display peptide library, (ii) the information about the three-dimensional structure of alpha-bungarotoxin/lead-peptide complex, and (iii) the amino acid sequence analysis of different AChRs.
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{{ABSTRACT_PUBMED_11381118}}
==About this Structure==
==About this Structure==
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1HAA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAA OCA].
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1HAA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAA OCA].
==Reference==
==Reference==
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[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:37:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:53:40 2008''

Revision as of 04:53, 1 July 2008

Image:1haa.png

Template:STRUCTURE 1haa

A BETA-HAIRPIN STRUCTURE IN A 13-MER PEPTIDE THAT BINDS A-BUNGAROTOXIN WITH HIGH AFFINITY AND NEUTRALIZES ITS TOXICITY

Template:ABSTRACT PUBMED 11381118

About this Structure

1HAA is a Protein complex structure of sequences from Bungarus multicinctus. Full experimental information is available from OCA.

Reference

A beta -hairpin structure in a 13-mer peptide that binds alpha -bungarotoxin with high affinity and neutralizes its toxicity., Scherf T, Kasher R, Balass M, Fridkin M, Fuchs S, Katchalski-Katzir E, Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6629-34. Epub 2001 May 29. PMID:11381118

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