Naslov
Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin

Autori
Wlodarski, Tomasz ; Žagrović, Bojan

Izvornik
Proceedings of the National Academy of Sciences of the United States of America (0027-8424) 106 (2009), 46; 19346-19351

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
ubiquitin binding; protein recognition; Kolmogorov–Smirnov test

Sažetak
Noncovalent binding interactions between proteins are the central physicochemical phenomenon underlying biological signaling and functional control on the molecular level. Here, we perform an extensive structural analysis of a large set of bound and unbound ubiquitin conformers and study the level of residual induced fit after conformational selection in the binding process. We show that the region surrounding the binding site in ubiquitin undergoes conformational changes that are significantly more pronounced compared with the whole molecule on average. We demonstrate that these induced-fit structural adjustments are comparable in magnitude to conformational selection. Our final model of ubiquitin binding blends conformational selection with the subsequent induced fit and provides a quantitative measure of their respective contributions.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Biologija

POVEZANOST RADA