| Literature DB >> 32510467 |
Alexandr Bolgov1, Svetlana Korban1, Dmitrii Luzik2, Vladimir Zhemkov1, Meewhi Kim3, Olga Rogacheva2, Ilya Bezprozvanny1.
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.Entities:
Keywords: Grb2; SH3 domain; adaptor protein; growth factor receptor-bound protein 2
Mesh:
Substances:
Year: 2020 PMID: 32510467 PMCID: PMC7278502 DOI: 10.1107/S2053230X20007232
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056