Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin (CROSBI ID 557396)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa
Podaci o odgovornosti
Zagrovic, 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.
conformational selection; induced fit; ubiquitin
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Podaci o prilogu
2009.
objavljeno
Podaci o matičnoj publikaciji
Podaci o skupu
EMBO YIP meeting
pozvano predavanje
01.01.2009-01.01.2009
Istanbul, Turska