The calmodulin-binding domain of the inducible (macrophage) nitric oxide synthase.

Détails

ID Serval
serval:BIB_57AC11F8A013
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The calmodulin-binding domain of the inducible (macrophage) nitric oxide synthase.
Périodique
European journal of biochemistry / FEBS
Auteur(s)
Anagli J., Hofmann F., Quadroni M., Vorherr T., Carafoli E.
ISSN
0014-2956
Statut éditorial
Publié
Date de publication
11/1995
Peer-reviewed
Oui
Volume
233
Numéro
3
Pages
701-708
Langue
anglais
Résumé
A domain in the inducible, macrophage nitric oxide (NO) synthase has been selected as the putative calmodulin-binding site. The domain was synthesized as a peptide of 29 residues [P29, NO synthase-(504-532)-peptide], having the accepted hydrophobic/basic composition of calmodulin-binding domains and containing, like most of them, an aromatic amino acid at its N-terminus and a long chain aliphatic residue 12 amino acids downstream of it. A 34-residue peptide from the synthase sequence [P34, NO synthase-(499-532)-peptide], consisting of peptide P29 and of the five extra N-terminal amino acids, three of them basic, was also synthesized. Both peptides bound calmodulin in the presence as well as in the absence of Ca2+ (i.e. in the presence of excess EGTA). The KD of the binding in the presence of Ca2+ was < or = 1 nM. The binding affinity was lower, but still remarkably high in the presence of EGTA. The peptides counteracted the stimulation by calmodulin of a classical calmodulin-target enzyme, the Ca2+ pump of the plasma membrane.
Mots-clé
Amino Acid Sequence, Animals, Binding Sites, Calmodulin-Binding Proteins, Enzyme Induction, Macrophages, Molecular Sequence Data, Nitric Oxide Synthase, Rats, Sequence Alignment
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:46
Dernière modification de la notice
20/08/2019 15:11
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