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

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

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.
Original languageEnglish
JournalActa Crystallographica. Section D: Biological Crystallography
Volume59
Issue numberPt 12
Pages (from-to)2300-2
Number of pages3
ISSN0907-4449
DOIs
Publication statusPublished - 2003

    Research areas

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

ID: 40318661