Dissociation constant of the cohesin–dockerin interaction in anaerobic bacteria

Range <10^-11 M
Organism bacteria
Reference Stahl SW et al., Single-molecule dissection of the high-affinity cohesin-dockerin complex. Proc Natl Acad Sci U S A. 2012 Dec 11 109(50):20431-6. doi: 10.1073/pnas.1211929109 p.20431 right column top paragraphPubMed ID23188794
Comments P.20431 right column top paragraph: "The cohesin–dockerin interaction is among the highest affinity protein–protein interactions known, with a dissociation constant of <10^−11 M. Dockerins form their binding interface to the cohesin through a duplicated 22-residue calcium binding loop–helix F-hand motif. The dockerin modules are believed to bind to cohesins in two different configurations, a phenomenon referred to as the dual binding mode (ref 2), shown in Fig. 1B. The two binding modes are thought to have evolved as a way to increase the conformational space for enzymes bound to the extracellular scaffoldin, and provide alternative modes of interaction between the enzymes and substrate (ref 3)."
Entered by Uri M
ID 114328