GroEL "relaxed" conformation

One end of GroEL is transiently blocked by the co-chaperonin GroES, an assembly of 10,000-MW subunits. (b) In the absence of ATP or presence of ADP GroEL exists in a "tight" conformational state that binds partly folded or misfolded proteins. Binding of ATP shifts GroEL to a more open, "relaxed" state, which releases the folded protein. See text for details. [Part (b) from A. Roseman et al., 1996, Cell 87:241; courtesy of H. Saibil.]

Was this article helpful?

0 0
Your Heart and Nutrition

Your Heart and Nutrition

Prevention is better than a cure. Learn how to cherish your heart by taking the necessary means to keep it pumping healthily and steadily through your life.

Get My Free Ebook

Post a comment