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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1016/j.str.2006.09.013

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Structural Biology
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Feller, SM More by this author
Journal:
Structure (London, England : 1993)
Volume:
14
Issue:
12
Pages:
1741-1753
Publication date:
2006-12-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:fefae753-327c-44ec-9282-ce8ea6b76b14
Source identifiers:
30485
Local pid:
pubs:30485

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