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Journal article

Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.

Abstract:

The SH2 domain of cytoplasmic tyrosine kinases can enhance catalytic activity and substrate recognition, but the molecular mechanisms by which this is achieved are poorly understood. We have solved the structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specialized for positive signaling. In its active conformation, the SH2 domain tightly interacts with the kinase N-terminal lobe and positions the kinase alphaC helix in an active configuration through e...

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Publication status:
Published

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Publisher copy:
10.1016/j.cell.2008.07.047

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
Journal:
Cell More from this journal
Volume:
134
Issue:
5
Pages:
793-803
Publication date:
2008-09-01
DOI:
EISSN:
1097-4172
ISSN:
0092-8674
Language:
English
Keywords:
Pubs id:
pubs:34373
UUID:
uuid:acccff65-308b-4636-a0c7-ef0464d5525d
Local pid:
pubs:34373
Source identifiers:
34373
Deposit date:
2012-12-19

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