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Crystal structure of the SH3 domain of growth factor receptor-bound protein 2. / Bolgov, Alexandr; Korban, Svetlana; Luzik, Dmitrii; Zhemkov, Vladimir; Kim, Meewhi; Rogacheva, Olga; Bezprozvanny, Ilya.

In: Acta crystallographica. Section F, Structural biology communications, Vol. 76, No. Pt 6, 29.05.2020, p. 263-270.

Research output: Contribution to journal › Article › peer-review

Harvard

Bolgov, A, Korban, S, Luzik, D, Zhemkov, V, Kim, M, Rogacheva, O & Bezprozvanny, I 2020, 'Crystal structure of the SH3 domain of growth factor receptor-bound protein 2', Acta crystallographica. Section F, Structural biology communications, vol. 76, no. Pt 6, pp. 263-270. https://doi.org/10.1107/S2053230X20007232

APA

Bolgov, A., Korban, S., Luzik, D., Zhemkov, V., Kim, M., Rogacheva, O., & Bezprozvanny, I. (2020). Crystal structure of the SH3 domain of growth factor receptor-bound protein 2. Acta crystallographica. Section F, Structural biology communications, 76(Pt 6), 263-270. https://doi.org/10.1107/S2053230X20007232

Vancouver

Bolgov A, Korban S, Luzik D, Zhemkov V, Kim M, Rogacheva O et al. Crystal structure of the SH3 domain of growth factor receptor-bound protein 2. Acta crystallographica. Section F, Structural biology communications. 2020 May 29;76(Pt 6):263-270. https://doi.org/10.1107/S2053230X20007232

Author

Bolgov, Alexandr ; Korban, Svetlana ; Luzik, Dmitrii ; Zhemkov, Vladimir ; Kim, Meewhi ; Rogacheva, Olga ; Bezprozvanny, Ilya. / Crystal structure of the SH3 domain of growth factor receptor-bound protein 2. In: Acta crystallographica. Section F, Structural biology communications. 2020 ; Vol. 76, No. Pt 6. pp. 263-270.

BibTeX

@article{5697a7dfc9d0401ea93a2e2ecbd40e9a,
title = "Crystal structure of the SH3 domain of growth factor receptor-bound protein 2",
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 {\AA} 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 {\AA} compared with 3.1 {\AA} 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.",
keywords = "adaptor protein, Grb2, growth factor receptor-bound protein 2, SH3 domain, REFINEMENT, REFMAC5, LIGAND-BINDING, SOS, ADAPTER, KNOWLEDGE, HYDROGEN-BONDS, FAMILY",
author = "Alexandr Bolgov and Svetlana Korban and Dmitrii Luzik and Vladimir Zhemkov and Meewhi Kim and Olga Rogacheva and Ilya Bezprozvanny",
year = "2020",
month = may,
day = "29",
doi = "10.1107/S2053230X20007232",
language = "English",
volume = "76",
pages = "263--270",
journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",
issn = "2053-230X",
publisher = "Wiley-Blackwell",
number = "Pt 6",

}

RIS

TY - JOUR

T1 - Crystal structure of the SH3 domain of growth factor receptor-bound protein 2

AU - Bolgov, Alexandr

AU - Korban, Svetlana

AU - Luzik, Dmitrii

AU - Zhemkov, Vladimir

AU - Kim, Meewhi

AU - Rogacheva, Olga

AU - Bezprozvanny, Ilya

PY - 2020/5/29

Y1 - 2020/5/29

N2 - 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.

AB - 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.

KW - adaptor protein

KW - Grb2

KW - growth factor receptor-bound protein 2

KW - SH3 domain

KW - REFINEMENT

KW - REFMAC5

KW - LIGAND-BINDING

KW - SOS

KW - ADAPTER

KW - KNOWLEDGE

KW - HYDROGEN-BONDS

KW - FAMILY

UR - http://www.scopus.com/inward/record.url?scp=85086135312&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/902b6db6-d6a0-3875-aef3-23cd504a6309/

U2 - 10.1107/S2053230X20007232

DO - 10.1107/S2053230X20007232

M3 - Article

C2 - 32510467

AN - SCOPUS:85086135312

VL - 76

SP - 263

EP - 270

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

SN - 2053-230X

IS - Pt 6

ER -

ID: 60792360