| Autor: |
Adeleke Aguda, Sami Caner, Nham T. Nguyen, Gary D. Brayer, Amina Zoubeidi, Martin E. Gleave, Barbara Lelj-Garolla, Susan C. Moore |
| Rok vydání: |
2014 |
| Předmět: |
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| Zdroj: |
Acta Crystallographica Section A Foundations and Advances. 70:C804-C804 |
| ISSN: |
2053-2733 |
| DOI: |
10.1107/s2053273314091955 |
| Popis: |
Human heat shock protein 27 (Hsp27) is an oligomeric and cell survival protein that has been associated with several cancers including prostrate and breast cancer. It's a known anti-apoptotic protein that functions as a molecular chaperone for several proteins. Hsp27 characteristically binds and stabilizes numerous partially unfolded proteins preventing their degradation, and has been shown to prevent actin polymerization in vitro. Several actin-binding residues involved in this interaction have been identified at the N-terminal loop and highly conserved alpha crystallin domains of Hsp27. Multiple assays have demonstrated that this hydrophobic actin-binding site is also involved in other protein binding. We therefore propose a common substrate-binding region on Hsp27 and present a model of Hsp27 binding to actin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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