Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin (CROSBI ID 157293)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Wlodarski, Tomasz ; Žagrović, Bojan
engleski
Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin
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.
ubiquitin binding; protein recognition; Kolmogorov–Smirnov test
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Podaci o izdanju
106 (46)
2009.
19346-19351
objavljeno
0027-8424
10.1073/pnas.0906966106