Acta biochimica et biophysica Sinica, 2012-04, Vol.44 (4), p.300-306
2012
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90
- Ist Teil von
- Acta biochimica et biophysica Sinica, 2012-04, Vol.44 (4), p.300-306
- Ort / Verlag
- China
- Erscheinungsjahr
- 2012
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- The activation of molecular chaperone heat-shock protein 90 （Hsp90） is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein. Here, we have determined three crystal structures of the N-ter- minal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90. Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1672-9145eISSN: 1745-7270DOI: 10.1093/abbs/gms001Titel-ID: cdi_proquest_miscellaneous_963833238
- Format
- –
- Schlagworte
- Adenosine Triphosphate - analogs & derivatives, Adenosine Triphosphate - chemistry, Adenosine Triphosphate - metabolism, Amino Acid Sequence, ATP, Binding Sites - genetics, Crystallography, X-Ray, HSP90, HSP90 Heat-Shock Proteins - chemistry, HSP90 Heat-Shock Proteins - genetics, HSP90 Heat-Shock Proteins - metabolism, Humans, Hydrolysis, Models, Molecular, Molecular Sequence Data, N-末端, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid, 水解机制, 激活, 热休克蛋白90, 结构洞