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


Autoria(s): Dar I.; Bonny C.; Pedersen J.T.; Gajhede M.; Kristensen O.
Data(s)

2003

Resumo

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.

Identificador

http://serval.unil.ch/?id=serval:BIB_75E092243BFC

isbn:0907-4449

pmid:14646101

doi:10.1107/S0907444903020304

isiid:000186884000041

Idioma(s)

en

Fonte

Acta crystallographica. Section D, Biological crystallography, vol. 59, no. Pt 12, pp. 2300-2

Palavras-Chave #Crystallization; Crystallography, X-Ray; Nuclear Proteins; Recombinant Fusion Proteins; Selenomethionine; Trans-Activators; src Homology Domains
Tipo

info:eu-repo/semantics/article

article