| Full text | |
| Author(s): |
Sanches, Karoline
[1]
;
Caruso, Icaro P.
[1, 2, 3]
;
Almeida, Fabio C. L.
[2, 3]
;
Melo, Fernando A.
[1]
Total Authors: 4
|
| Affiliation: | [1] Sao Paulo State Univ UNESP, CMIB, Dept Phys, Sao Paulo - Brazil
[2] Univ Fed Rio de Janeiro, Inst Med Biochem IBqM, Rio De Janeiro - Brazil
[3] Univ Fed Rio de Janeiro, Ctr Struct Biol & Bioimaging CENABIO, Natl Ctr Nucl Magnet Resonance, Rio De Janeiro - Brazil
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | BIOMOLECULAR NMR ASSIGNMENTS; v. 13, n. 2, p. 295-298, OCT 2019. |
| Web of Science Citations: | 0 |
| Abstract | |
Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein composed of three domains, an N-terminal SH3 (nSH3), SH2 and a C-terminal SH3 (cSH3) domains. This multi-domain protein has been reported to be a key factor in many signaling pathways related to controlling cell survival, differentiation, and growth. The Grb2-SH2 domain has been a focus for the study of the interaction with peptides and small molecules to act as inhibitors in uncontrolled cell growth, and consequently inhibit tumor proliferation. Here we describe the almost complete assignment of the free SH2 domain at pH 7. This work prepares the ground for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. TalosN secondary structure prediction showed great similarity with the available structures in the PDB. (AU) | |
| FAPESP's process: | 14/17630-0 - Functional studies of tyrosine kinase fibroblast growth factor receptor (FGFR2), the adapter growth factor receptor-Bound protein 2 (Grb2) and tyrosine phosphatase SHP2 |
| Grantee: | Fernando Alves de Melo |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 09/53989-4 - Acquisition of a nuclear magnetic resonance spectrometer for studies of biomolecules |
| Grantee: | Raghuvir Krishnaswamy Arni |
| Support Opportunities: | Multi-user Equipment Program |