Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1
- Authors
- Song, JinSue; Park, Joon Kyu; Lee, Jae-Jin; Choi, Yun-Seok; Ryu, Kyoung-Seok; Kim, Jae-Hong; Kim, Eunhee; Lee, Kong-Joo; Jeon, Young-Ho; Kim, Eunice EunKyeong
- Issue Date
- 11월-2009
- Publisher
- WILEY
- Citation
- PROTEIN SCIENCE, v.18, no.11, pp.2265 - 2276
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROTEIN SCIENCE
- Volume
- 18
- Number
- 11
- Start Page
- 2265
- End Page
- 2276
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/119040
- DOI
- 10.1002/pro.237
- ISSN
- 0961-8368
- Abstract
- 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.
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