Crystal Structure of the SH3 Domain of Growth Factor Receptor-bound Protein 2

Overview

Journal Acta Crystallogr F Struct Biol Commun

Specialty Chemistry

Date 2020 Jun 9

PMID 32510467

Citations 4

Authors

Alexandr Bolgov

Svetlana Korban

Dmitrii Luzik

Vladimir Zhemkov

Meewhi Kim

Olga Rogacheva

Ilya Bezprozvanny

Affiliations

Soon will be listed here.

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.

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