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TitleCooperative Domain Formation by Homologous Motifs in HOIL-1L and SHARPIN Plays A Crucial Role in LUBAC Stabilization.
Journal, issue, pagesCell Rep, Vol. 23, Page 1192-1204, Year 2018
Publish dateJul 31, 2017 (structure data deposition date)
AuthorsFujita, H. / Tokunaga, A. / Shimizu, S. / Whiting, A.L. / Aguilar-Alonso, F. / Takagi, K. / Walinda, E. / Sasaki, Y. / Shimokawa, T. / Mizushima, T. ...Fujita, H. / Tokunaga, A. / Shimizu, S. / Whiting, A.L. / Aguilar-Alonso, F. / Takagi, K. / Walinda, E. / Sasaki, Y. / Shimokawa, T. / Mizushima, T. / Ohki, I. / Ariyoshi, M. / Tochio, H. / Bernal, F. / Shirakawa, M. / Iwai, K.
External linksCell Rep / PubMed:29694895
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-5y3t:
Crystal structure of hetero-trimeric core of LUBAC: HOIP double-UBA complexed with HOIL-1L UBL and SHARPIN UBL
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsLIGASE / HOIP / HOIL-1L / SHARPIN / Linear-Ubiquitin Assembly Complex / NF-KB Activation / LUBAC Tethering Motif / LUBAC Stabilization

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