Abstract
This study presents the crystal structure of the N-terminal SH3 (SH3N) domain of growth factor receptor-bound protein 2 (Grb2) at 2.5 Å resolution. Grb2 is a small (215-amino-acid) adaptor protein that is widely expressed and involved in signal transduction/cell communication. The crystal structure of full-length Grb2 has previously been reported (PDB entry 1gri). The structure of the isolated SH3N domain is consistent with the full-length structure. The structure of the isolated SH3N domain was solved at a higher resolution (2.5 Å compared with 3.1 Å for the previously deposited structure) and made it possible to resolve some of the loops that were missing in the full-length structure. In addition, interactions between the carboxy-terminal region of the SH3N domain and the Sos1-binding sites were observed in the structure of the isolated domain. Analysis of these interactions provided new information about the ligand-binding properties of the SH3N domain of Grb2.
Original language | English (US) |
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Pages (from-to) | 263-270 |
Number of pages | 8 |
Journal | Acta Crystallographica Section F:Structural Biology Communications |
Volume | 76 |
DOIs | |
State | Published - May 29 2020 |
Keywords
- Grb2
- SH3 domain
- adaptor protein
- growth factor receptor-bound protein 2
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics