The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal.

Journal article

CRKL plays essential roles in cell signaling. It consists of an N-terminal SH2 domain followed by two SH3 domains. SH2 and SH3N bind to signaling proteins, but the function of the SH3C domain has remained largely enigmatic. We show here that the SH3C of CRKL forms homodimers in protein crystals and in solution. Evidence for dimer formation of full-length CRKL is also presented. In the SH3C dimer, a nuclear export signal (NES) is mostly buried under the domain surface. The same is true for a m...

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Authors: Harkiolaki, M; Gilbert, R; Jones, E; Feller, S

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 14
• Issue: 12
• Pages: 1741-1753
• Publication date: 2006-12-01
• DOI: 10.1016/j.str.2006.09.013
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Humans; Models, Molecular; Protein Structure, Secondary; Surface Properties; Nuclear Proteins; Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Molecular Sequence Data; Hela Cells; Sequence Homology, Amino Acid; Antigens, CD34; Nuclear Export Signals; src Homology Domains; Protein Binding; Dimerization