The Three-Dimensional Solution Structure of the Src Homology Domain-2 of the Growth Factor Receptor-Bound Protein-2
- 1 January 1998
- journal article
- research article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 11 (2) , 153-164
- https://doi.org/10.1023/A:1008250309874
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Protein modules and signalling networksNature, 1995
- Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniquesJournal of Biomolecular NMR, 1994
- Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 1993
- Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lckNature, 1993
- Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.Proceedings of the National Academy of Sciences, 1992
- Three-dimensional solution structure of the src homology 2 domain of c-ablCell, 1992
- The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signalingCell, 1992
- The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structuresProtein Science, 1992
- Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbonsProteins-Structure Function and Bioinformatics, 1991
- Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonanceJournal of Molecular Biology, 1983