6SDF

N-terminal SH3 domain of Grb2 protein

Summary for 6SDF

• Entry DOI: 10.2210/pdb6sdf/pdb
• Descriptor: Growth factor receptor-bound protein 2, (4S)-2-METHYL-2,4-PENTANEDIOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: growth factor, grb2, sh3-domain, signaling protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 14702.83

Authors

Bolgov, A.A.,Korban, S.A.,Luzik, D.A.,Rogacheva, O.N.,Zhemkov, V.A.,Kim, M.,Skrynnikov, N.R.,Bezprozvanny, I.B. (deposition date: 2019-07-26, release date: 2020-01-29, Last modification date: 2024-01-24)

Primary citation

Bolgov, A.,Korban, S.,Luzik, D.,Zhemkov, V.,Kim, M.,Rogacheva, O.,Bezprozvanny, I.
Crystal structure of the SH3 domain of growth factor receptor-bound protein 2.
Acta Crystallogr.,Sect.F, 76:263-270, 2020

PubMed 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.

PubMed: 32510467
DOI: 10.1107/S2053230X20007232

Experimental method

X-RAY DIFFRACTION (2.5 Å)