Related ArticlesNMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain.
Biomol NMR Assign. 2019 Apr 26;:
Authors: Sanches K, Caruso ÍP, Almeida FCL, Melo FA
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.
PMID: 31028611 [PubMed - as supplied by publisher]
[NMR paper] Rapid identification of ligand-binding sites by using an assignment-free NMR approach.
Rapid identification of ligand-binding sites by using an assignment-free NMR approach.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Rapid identification of ligand-binding sites by using an assignment-free NMR approach.
J Med Chem. 2013 Oct 30;
Authors: Kodama Y, Takeuchi K, Shimba N, Ishikawa K, Suzuki EI, Shimada I, Takahashi H
Abstract
In this study, we developed an assignment-free approach for rapid identification of ligand-binding sites in target...
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11-01-2013 07:39 PM
[NMR paper] Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Sci Rep. 2013;3:2913
Authors: Ogura K, Okamura H
Abstract
Growth factor receptor-bound protein 2 (Grb2) is a small adapter protein composed of a single SH2 domain flanked by two SH3 domains. The...
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10-10-2013 09:38 PM
[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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11-22-2012 11:49 AM
[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Related Articles Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Biochemistry. 2004 Aug 17;43(32):10393-9
Authors: Lysek DA, Wüthrich K
Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified,...
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11-24-2010 10:01 PM
[NMR paper] Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronu
Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronuclear NMR spectroscopy.
Related Articles Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronuclear NMR spectroscopy.
J Biomol NMR. 1996 Mar;7(2):89-98
Authors: Wang YS, Frederick AF, Senior MM, Lyons BA, Black S, Kirschmeier P, Perkins LM, Wilson O
The growth factor receptor-bound protein-2 (Grb-2) is an adaptor protein that mediates signal transduction pathways. Chemical shift assignments were obtained for the SH2 domain of...
[NMR paper] 1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-termin
1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X.
Related Articles 1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X.
Biochemistry. 1990 Sep 4;29(35):8111-8
Authors: Selander M, Persson E, Stenflo J, Drakenberg T
Blood coagulation factor X is composed of discrete domains, two of which are homologous to the epidermal growth factor (EGF). The...
NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain.
Linear Mode
