The N-Terminal End of the Catalytic Domain of Src Kinase Hck Is a Conformational Switch Implicated in Long-Range Allosteric Regulation
- 1 November 2005
- Vol. 13 (11) , 1715-1723
- https://doi.org/10.1016/j.str.2005.09.005
Abstract
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This publication has 36 references indexed in Scilit:
- Evolutionarily conserved networks of residues mediate allosteric communication in proteinsNature Structural & Molecular Biology, 2002
- Extension to the weighted histogram analysis method: combining umbrella sampling with free energy calculationsPublished by Elsevier ,2001
- All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of ProteinsThe Journal of Physical Chemistry B, 1998
- Crystal structure of the Src family tyrosine kinase HckNature, 1997
- Three-dimensional structure of the tyrosine kinase c-SrcNature, 1997
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Finite representation of an infinite bulk system: Solvent boundary potential for computer simulationsThe Journal of Chemical Physics, 1994
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Ligand binding and internal equilibiums in proteinsBiochemistry, 1972
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965