Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics.
By V. P. Chuprina, J. Rullmann, R. Lamerichs, J. Boom, Rolf Boelens, R. Kaptein. 1994
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- M. V. van Dijk
- Alexandre M. J. J. Bonvin
- Pauline Crystal Ng
- Steven Henikoff
- A. V. van Dijk
- V. Hsu
- Rolf Boelens
- Yana Bromberg
Citations in the corpus
- Pushing the limits of what is achievable in protein–DNA docking: benchmarking HADDOCK’s performance (2010, methodology): “The protocol was initially tested by docking the unbound structures of three monomeric transcription factors to their respective operator half-sites [phage 434 Cro (21), phage (cid:2) Arc (22) and Escherichia coli Lac (23)].”
- Predicting deleterious amino acid substitutions. (2001, background): “In general, SIFT predicts better than substitution matrices on HIV-1 protease mutation data; with careful selection of sequences and comparison of structures, performance can be improved further.”
- Information-driven protein–DNA docking using HADDOCK: it is a matter of flexibility (2006, background): “The PDB entry codes of the respective complexes and their unbound components are as follows: 3CRO, crystal structures of the Cro/O1R complex (19); 1ZUG, NMR ensemble of the unbound Cro monomer (23); 1LCC, NMR ensemble of the Lac/O1 complex (24); 1LQC, NMR ensemble of the unbound monomer of the Lac h”