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Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1
- Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1
- Song J.; Joon K.P.; Lee J.-J.; Choi Y.-S.; Ryu K.-S.; Kim J.-H.; Kim E.; Lee K.-J.; Jeon Y.-H.; Kim E.E.
- Ewha Authors
- SCOPUS Author ID
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- Protein Science
- Protein Science vol. 18, no. 11, pp. 2265 - 2276
- SCI; SCIE; SCOPUS
- Document Type
- Fas-associated factor (FAF)-1 is a multidomain protein that was first identified as a member of the Fas death-inducing signaling complex, but later found to be involved in various biological processes. Although the exact mechanisms are not clear, FAF1 seems to play an important role in cancer, asbestos-induced mesotheliomas, and Parkinson's disease. It interacts with polyubiquitinated proteins, Hsp70, and p97/VCP (valosin-containing protein), in addition to the proteins of the Fas-signaling pathway. We have determined the crystal structure of the ubiquitin-associated domain of human FAF1 (hFAF1-UBA) and examined its interaction with ubiquitin and ubiquitin-like proteins using nuclear magnetic resonance. hFAF1-UBA revealed a canonical three-helical bundle that selectively binds to mono- and di-ubiquitin (Lys48-linked), but not to SUMO-1 (small ubiquitin-related modifier 1) or NEDD8 (neural precursor cell expressed, developmentally down-regulated 8). The interaction between hFAF1-UBA and di-ubiquitin involves hydrophobic interaction accompanied by a transition in the di-ubiquitin conformation. These results provide structural insight into the mechanism of polyubiquitin recognition by hFAF1-UBA. Published by Wiley-Blackwell. © 2009 The Protein Society.
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