Author:
Sakurai Shunya,Shimizu Toshiyuki,Ohto Umeharu
Abstract
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 Å 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.
Funder
Ministry of Education, Culture, Sports, Science and Technology
Core Research for Evolutional Science and Technology
Japan Science and Technology Agency
Mochida Memorial Foundation for Medical and Pharmaceutical Research
Daiichi Sankyo Foundation of Life Science
Uehara Memorial Foundation
Naito Foundation
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Cited by
4 articles.
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