A structural change occurs upon binding of syntaxin to SNAP-25.

Détails

ID Serval
serval:BIB_6516D65F8B32
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A structural change occurs upon binding of syntaxin to SNAP-25.
Périodique
Journal of Biological Chemistry
Auteur⸱e⸱s
Fasshauer D., Bruns D., Shen B., Jahn R., Brünger A.T.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
1997
Peer-reviewed
Oui
Volume
272
Numéro
7
Pages
4582-4590
Langue
anglais
Résumé
The highly conserved proteins syntaxin and SNAP-25 are part of a protein complex that is thought to play a key role in exocytosis of synaptic vesicles. Previous work demonstrated that syntaxin and SNAP-25 bind to each other with high affinity and that their binding regions are predicted to form coiled coils. Circular dichroism spectroscopy was used here to study the alpha-helicity of the individual proteins and to gain insight into structural changes associated with complex formation. Syntaxin displayed approximately 43% alpha-helical content. In contrast, the alpha-helical content of SNAP-25 was low under physiological conditions. Formation of the SNAP-25-syntaxin complex was associated with a dramatic increase in alpha-helicity. Interaction of a 90-residue NH2-terminal fragment of SNAP-25 comprising the minimal syntaxin binding domain lead to a similar but less pronounced increase in alpha-helicity. Single amino acid replacements in the putative hydrophobic core of this fragment with hydrophilic amino acids abolished the induced structural change and disrupted the interaction monitored by binding assays. Replacements with hydrophobic residues had no effect. Our findings are consistent with induced coiled coil formation upon binding of syntaxin and SNAP-25.
Mots-clé
Amino Acid Sequence, Animals, Circular Dichroism, Hydrogen-Ion Concentration, Leeches, Membrane Proteins/chemistry, Membrane Proteins/genetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Nerve Tissue Proteins/metabolism, Osmolar Concentration, Protein Binding, Protein Conformation, Qa-SNARE Proteins, Recombinant Proteins/chemistry, Recombinant Proteins/genetics, Sequence Homology, Amino Acid, Synaptosomal-Associated Protein 25
Pubmed
Web of science
Création de la notice
15/09/2011 10:46
Dernière modification de la notice
20/08/2019 15:21
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