High resolution crystal structures of the p120 RasGAP SH3 domain

Détails

ID Serval
serval:BIB_FE02BBC473F7
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
High resolution crystal structures of the p120 RasGAP SH3 domain
Périodique
Biochemical and Biophysical Research Communications
Auteur(s)
Ross  B., Kristensen  O., Favre  D., Walicki  J., Kastrup  J. S., Widmann  C., Gajhede  M.
ISSN
0006-291X (Print)
Statut éditorial
Publié
Date de publication
02/2007
Volume
353
Numéro
2
Pages
463-8
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Feb 9
Résumé
X-ray structures of two crystal forms of the Src homology 3 domain (SH3) of the Ras GTPase activating protein (RasGAP) were determined at 1.5 and 1.8A resolution. The overall structure comprises a single domain with two tightly packed beta-sheets linked by a short helical segment. An important motif for peptide binding in other SH3 domains is not conserved in RasGAP. The RasGAP SH3 domain forms dimers in the crystal structures, which may provide new functional insight. The dimer interface involves residues also present in a peptide previously identified as an apoptotic sensitizer of tumor cells.
Mots-clé
Amino Acid Sequence Binding Sites Computer Simulation Crystallography Dimerization *Models, Chemical *Models, Molecular Molecular Sequence Data Protein Binding Protein Conformation p120 GTPase Activating Protein/*chemistry/*ultrastructure *src Homology Domains
Pubmed
Web of science
Création de la notice
24/01/2008 15:43
Dernière modification de la notice
20/08/2019 17:28
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