Solution structure of Grb2 reveals extensive flexibility necessary for target recognition
- 23 February 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 306 (3) , 527-537
- https://doi.org/10.1006/jmbi.2000.4396
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Signaling—2000 and BeyondCell, 2000
- Direct Determination of Changes of Interdomain Orientation on Ligation: Use of the Orientational Dependence of 15N NMR Relaxation in Abl SH(32)Biochemistry, 1999
- A Sos‐derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activityThe FASEB Journal, 1999
- [11] Fluorescence methods for studying equilibrium macromolecule-ligand interactionsPublished by Elsevier ,1997
- The Grb2-mSos1 Complex Binds Phosphopeptides with Higher Affinity than Grb2Published by Elsevier ,1996
- Enhanced Affinities and Specificities of Consolidated Ligands for the Src Homology (SH) 3 and SH2 Domains of Abelson Protein-tyrosine KinasePublished by Elsevier ,1995
- The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) constructStructure, 1995
- Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR RelaxationBiochemistry, 1994
- Biased combinatorial libraries: novel ligands for the SH3 domain of phosphatidylinositol 3-kinaseJournal of the American Chemical Society, 1993
- Surface, subunit interfaces and interior of oligomeric proteinsJournal of Molecular Biology, 1988