Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53 1 1Edited by M. F. Summers
- 1 November 2001
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 314 (3) , 563-575
- https://doi.org/10.1006/jmbi.2001.5140
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexesJournal of Molecular Biology, 2001
- Determination of three‐dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms Circumventing problems associated with foldingPublished by Wiley ,2001
- Structure of the FHA1 Domain of Yeast Rad53 and Identification of Binding Sites for both FHA1 and its Target Protein Rad9Journal of Molecular Biology, 2000
- II. Structure and specificity of the interaction between the FHA2 domain of rad53 and phosphotyrosyl peptides†,1Journal of Molecular Biology, 2000
- SMART: a web-based tool for the study of genetically mobile domainsNucleic Acids Research, 2000
- Structure and function of a new phosphopeptide-binding domain containing the FHA2 of rad53Journal of Molecular Biology, 1999
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- A pulsed field gradient isotope‐filtered 3D 13C HMQC‐NOESY experiment for extracting intermolecular NOE contacts in molecular complexesFEBS Letters, 1994
- Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 1993
- Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectraJournal of Magnetic Resonance (1969), 1988