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

Details

Serval ID
serval:BIB_75E092243BFC
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein.
Journal
Acta crystallographica. Section D, Biological crystallography
Author(s)
Dar I., Bonny C., Pedersen J.T., Gajhede M., Kristensen O.
ISSN
0907-4449
Publication state
Published
Issued date
2003
Peer-reviewed
Oui
Volume
59
Number
Pt 12
Pages
2300-2
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Abstract
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.
Keywords
Crystallization, Crystallography, X-Ray, Nuclear Proteins, Recombinant Fusion Proteins, Selenomethionine, Trans-Activators, src Homology Domains
Pubmed
Web of science
Create date
25/01/2008 14:15
Last modification date
20/08/2019 14:33
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