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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Selenomethionine / chemistry
  • Trans-Activators / chemistry*
  • Trans-Activators / genetics
  • src Homology Domains

Substances

  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Trans-Activators
  • Selenomethionine