Identification of substrate binding site of GroEL minichaperone in solution
نویسندگان
چکیده
منابع مشابه
Identification of substrate binding site of cyclin-dependent kinase 5.
Cyclin-dependent kinase 5 (CDK5), unlike other CDKs, is active only in neuronal cells where its neuron-specific activator p35 is present. However, it phosphorylates serines/threonines in S/TPXK/R-type motifs like other CDKs. The tail portion of neurofilament-H contains more than 50 KSP repeats, and CDK5 has been shown to phosphorylate S/T specifically only in KS/TPXK motifs, indicating highly s...
متن کاملMultivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL
The chaperonin GroEL binds nonnative substrate protein in the central cavity of an open ring through exposed hydrophobic residues at the inside aspect of the apical domains and then mediates productive folding upon binding ATP and the cochaperonin GroES. Whether nonnative proteins bind to more than one of the seven apical domains of a GroEL ring is unknown. We have addressed this using rings wi...
متن کاملProtein Substrate Binding Induces Conformational Changes in the Chaperonin GroEL
Chaperonins are molecules that assist proteins during folding and protect them from irreversible aggregation. We studied the chaperonin GroEL and its interaction with the enzyme human carbonic anhydrase II (HCA II), which induces unfolding of the enzyme. We focused on conformational changes that occur in GroEL during formation of the GroEL-HCA II complex. We measured the rate of GroEL cysteine ...
متن کاملThe substrate binding site of pepsin.
In earlier reports from this laboratory, a series of new synthetic substrates for pepsin was described.'-' These compounds are of the general type Z-His-X-YOAI\e4 where X and Y are the residues of amino acids such as L-phenylalanine, p-nitro-L-phenylalanine, L-tyrosine, L-tryptophan, and L-leucine; the enzymic action is limited to the cleavage of the X-Y bond. One of the substrate analogues pre...
متن کاملThe Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven-membered rings of GroEL plays an important role in regulating binding and release of folding substrates and of the small chaperonin GroES. Using cryo-electron microscopy, we have o...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1999
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.39.s157_3