Prodromou, C., Roe, S.M., Piper, P.W., Pearl, L.H.ĭepartment of Biochemistry and Molecular Biology, University College London, United Kingdom. A Molecular Clamp in the Crystal Structure of the N-Terminal Domain of the Yeast Hsp90 Chaperone While there are a number of mechanisms in place to achieve this, one of the most common is the Hsp70/Hsp90 molecular chaperone system (Taipale et al., 2010).These results finally resolve the question of the direct involvement of ATP in Hsp90 function. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. Diversity, Equity, Inclusion, and Access The heat shock protein 90 (HSP90) chaperones represent some 1-2 of all cellular protein and are key players in protein quality control in cells.Citation, Usage, Privacy Policies, Logo Hsp90 is an abundant molecular chaperone essential to the establishment of many cellular regulation and signal transduction systems, but remains one of the.Biologically Interesting Molecule Reference Dictionary (BIRD).
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |