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

作者信息

Dar Imran, Bonny Christophe, Pedersen Jan Torleif, Gajhede Michael, Kristensen Ole

机构信息

Structural Chemistry Group, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100, Denmark.

出版信息

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2300-2. doi: 10.1107/s0907444903020304. Epub 2003 Nov 27.

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.

摘要

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