3ZM9

The mechanism of allosteric coupling in choline kinase a1 revealed by a rationally designed inhibitor

Summary for 3ZM9

• Entry DOI: 10.2210/pdb3zm9/pdb
• Descriptor: CHOLINE KINASE ALPHA, 1-(4-(4-(4-((6-amino-9H-purin-9-yl)methyl)phenyl)butyl)benzyl)-4- (dimethylamino)pyridinium (3 entities in total)
• Functional Keywords: transferase, negative cooperativity, allosteric mechanism, elastic network analysis
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P35790
• Total number of polymer chains: 2
• Total formula weight: 90894.19

Authors

Sahun-Roncero, M.,Rubio-Ruiz, B.,Saladino, G.,Conejo-Garcia, A.,Espinosa, A.,Velazquez-Campoy, A.,Gervasio, F.L.,Entrena, A.,Hurtado-Guerrero, R. (deposition date: 2013-02-06, release date: 2013-02-27, Last modification date: 2023-12-20)

Primary citation

Sahun-Roncero, M.,Rubio-Ruiz, B.,Saladino, G.,Conejo-Garcia, A.,Espinosa, A.,Velazquez-Campoy, A.,Gervasio, F.L.,Entrena, A.,Hurtado-Guerrero, R.
The Mechanism of Allosteric Coupling in Choline Kinase A1 Revealed by a Rationally Designed Inhibitor
Angew.Chem.Int.Ed.Engl., 52:4582-, 2013

PubMed Abstract: Applying a CHOK hold: Combined experimental and computational studies of the binding mode of a rationally designed inhibitor of the dimeric choline kinase α1 (CHOKα1) explain the molecular mechanism of negative cooperativity (see scheme) 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.

PubMed: 23441033
DOI: 10.1002/ANIE.201209660

Experimental method

X-RAY DIFFRACTION (1.9 Å)