Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein.
Data(s) |
2003
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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 |