Structural basis for specific cleavage of Lys63-linked polyubiquitin chains by Trabid
Project/Area Number |
22770099
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | The University of Tokyo |
Principal Investigator |
SATO Yusuke 東京大学, 放射光連携研究機構, 助教 (50568061)
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Project Period (FY) |
2010 – 2011
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Project Status |
Completed (Fiscal Year 2011)
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Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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Keywords | X線結晶解析 / X線結晶構造解析 / ユビキチン / NF-κB |
Research Abstract |
We prepared the mouse, zebrafish and fly Trabid OTU domain and screened against 500 crystallization conditions. However, the OTU domains of Trabid were not crystallized. On the other hand, we determined the crystal structure of the HOIL-1L NZF domain in complex with linear di-ubiquitin. Together with structure based mutagenesis experiments our structure reveals the mechanism for specific recognition of linear chains by the HOL-1L NZF domain. This result was published in PNAS
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Report
(3 results)
Research Products
(6 results)
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[Journal Article] Specific recognition of linear ubiquitin chains by the Npl4 zinc finger(NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex2011
Author(s)
Sato, Y., Fujita, H., Yoshikawa, A., Yamashita, M., Yamagata, A., Kaiser, S. E., Iwai, K., Fukai, S
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Journal Title
Proceedings of National Academy of Science United States of America
Volume: 108巻
Issue: 51
Pages: 20520-20525
DOI
Related Report
Peer Reviewed
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