Structural highlights
Publication Abstract from PubMed
Applying a CHOK hold: Combined experimental and computational studies of the binding mode of a rationally designed inhibitor of the dimeric choline kinase alpha1 (CHOKalpha1) explain the molecular mechanism of negative cooperativity and how the monomers are connected. The results give insight into how the symmetry of the dimer can be partially conserved despite a lack of conservation in the static crystal structures.
The Mechanism of Allosteric Coupling in Choline Kinase alpha1 Revealed by the Action of a Rationally Designed Inhibitor.,Sahun-Roncero M, Rubio-Ruiz B, Saladino G, Conejo-Garcia A, Espinosa A, Velazquez-Campoy A, Gervasio FL, Entrena A, Hurtado-Guerrero R Angew Chem Int Ed Engl. 2013 Feb 25. doi: 10.1002/anie.201209660. PMID:23441033[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sahun-Roncero M, Rubio-Ruiz B, Saladino G, Conejo-Garcia A, Espinosa A, Velazquez-Campoy A, Gervasio FL, Entrena A, Hurtado-Guerrero R. The Mechanism of Allosteric Coupling in Choline Kinase alpha1 Revealed by the Action of a Rationally Designed Inhibitor. Angew Chem Int Ed Engl. 2013 Feb 25. doi: 10.1002/anie.201209660. PMID:23441033 doi:http://dx.doi.org/10.1002/anie.201209660
