- 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 ...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1093/emboj/cdg258
-
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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
- Language:
- English
- Keywords:
- Copyright date:
- 2003
Journal article
Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76.
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