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.

Язык оригиналаанглийский
Страницы (с-по)263-270
Число страниц8
ЖурналActa crystallographica. Section F, Structural biology communications
Номер выпускаPt 6
СостояниеОпубликовано - 29 мая 2020

    Предметные области Scopus

  • Физика конденсатов
  • Генетика
  • Биофизика
  • Структурная биология
  • Биохимия

ID: 60792360