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 languageEnglish
Pages (from-to)263-270
Number of pages8
JournalActa crystallographica. Section F, Structural biology communications
Issue numberPt 6
StatePublished - 29 May 2020

    Research areas

  • adaptor protein, Grb2, growth factor receptor-bound protein 2, SH3 domain, REFINEMENT, REFMAC5, LIGAND-BINDING, SOS, ADAPTER, KNOWLEDGE, HYDROGEN-BONDS, FAMILY

    Scopus subject areas

  • Condensed Matter Physics
  • Genetics
  • Biophysics
  • Structural Biology
  • Biochemistry

ID: 60792360