Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein.
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.
Dar
Imran
I
Structural Chemistry Group, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100, Denmark.
Bonny
Christophe
C
Pedersen
Jan Torleif
JT
Gajhede
Michael
M
Kristensen
Ole
O
D003460:Crystallization; D018360:Crystallography, X-Ray; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D012645:Selenomethionine / Q000737:chemistry; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics; D018909:src Homology Domains
D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; D015534:Trans-Activators; D012645:Selenomethionine