Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 76, Issue -, Pages 326-333Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X20009012
Keywords
X-ray crystallography; autophagy; FYCO1; RUN domain; small GTPase binding
Funding
- Japanese Ministry of Education, Culture, Sports, Science and Technology [26711002, 19H00976]
- CREST, JST
- Takeda Science Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Daiichi Sankyo Foundation of Life Science
- Uehara Memorial Foundation
- Naito Foundation
- Grants-in-Aid for Scientific Research [19H00976, 26711002] Funding Source: KAKEN
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FYCO1 is a multidomain adaptor protein that plays an important role in autophagy by mediating the kinesin-dependent microtubule plus-end-directed transport of autophagosomes. FYCO1 contains a RUN domain, which is hypothesized to function as a specific effector for members of the Ras superfamily of small GTPases, but its role has not been well characterized and its interaction partner(s) have not been identified. Here, the crystal structure of the FYCO1 RUN domain was determined at 1.3 angstrom resolution. The overall structure of the FYCO1 RUN domain was similar to those of previously reported RUN domains. Detailed structural comparisons with other RUN domains and docking studies suggested a possible interaction interface of the FYCO1 RUN domain with small GTPases of the Ras superfamily.
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