Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein.

Détails

ID Serval
serval:BIB_75E092243BFC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein.
Périodique
Acta crystallographica. Section D, Biological crystallography
Auteur⸱e⸱s
Dar I., Bonny C., Pedersen J.T., Gajhede M., Kristensen O.
ISSN
0907-4449
Statut éditorial
Publié
Date de publication
2003
Peer-reviewed
Oui
Volume
59
Numéro
Pt 12
Pages
2300-2
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Résumé
IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.
Mots-clé
Crystallization, Crystallography, X-Ray, Nuclear Proteins, Recombinant Fusion Proteins, Selenomethionine, Trans-Activators, src Homology Domains
Pubmed
Web of science
Création de la notice
25/01/2008 15:15
Dernière modification de la notice
20/08/2019 15:33
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