Your browser version may not work well with NCBI's Web applications. More information
here...
-
Protein folding in the central cavity of the GroEL-GroES chaperonin complex.
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
The chaperonin GroEL is able to mediate protein folding in its central cavity. GroEL-bound dihydrofolate reductase assumes its native conformation when the GroES cofactor caps one end of the GroEL cylinder, thereby discharging the unfolded polypeptide into an enclosed cage. Folded dihydrofolate reductase emerges upon ATP-dependent GroES release. Other proteins, such as rhodanese, may leave GroEL after having attained a conformation that is committed to fold. Incompletely folded polypeptide rebinds to GroEL, resulting in structural rearrangement for another folding trial in the chaperonin cavity.
PMID: 8559246 [PubMed - indexed for MEDLINE]
-
Related Articles
-
Patient Drug Information
-
Methotrexate (Rheumatrex®, Trexall®)
Your doctor has ordered methotrexate to help treat your illness. Methotrexate comes as a tablet to take by mouth. Your doctor will tell you how often you should take methotrexate. The schedule depends on the condition y...