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Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76.

Abstract:

SH3 domains are protein recognition modules within many adaptors and enzymes. With more than 500 SH3 domains in the human genome, binding selectivity is a key issue in understanding the molecular basis of SH3 domain interactions. The Grb2-like adaptor protein Mona/Gads associates stably with the T-cell receptor signal transducer SLP-76. The crystal structure of a complex between the C-terminal SH3 domain (SH3C) of Mona/Gads and a SLP-76 peptide has now been solved to 1.7 A. The peptide lacks ...

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Publication status:
Published

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Publisher copy:
10.1093/emboj/cdg258

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Institution:
University of Oxford
Department:
Oxford, MSD, Structural Biology
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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Journal:
The EMBO journal
Volume:
22
Issue:
11
Pages:
2571-2582
Publication date:
2003-06-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:4e32497f-25bd-4829-899b-fe01b3982aaa
Source identifiers:
14645
Local pid:
pubs:14645

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