5B5W

Crystal structure of MOB1-LATS1 NTR domain complex

5B5W の概要

• エントリーDOI: 10.2210/pdb5b5w/pdb
• 関連するPDBエントリー: 5B5V
• 分子名称: MOB kinase activator 1B, Serine/threonine-protein kinase LATS1, ZINC ION (3 entities in total)
• 機能のキーワード: mob1 lats1 hippo pathway, metal binding protein-apotosis complex, metal binding protein/apotosis
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32037.11

構造登録者

KIM, S.-Y.,Tachioka, Y.,Mori, T.,Hakoshima, T. (登録日: 2016-05-24, 公開日: 2016-07-06, 最終更新日: 2023-11-08)

主引用文献

Kim, S.Y.,Tachioka, Y.,Mori, T.,Hakoshima, T.
Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway
Sci Rep, 6:28488-28488, 2016

PubMed Abstract: MOB1 protein is a key regulator of large tumor suppressor 1/2 (LATS1/2) kinases in the Hippo pathway. MOB1 is present in an autoinhibited form and is activated by MST1/2-mediated phosphorylation, although the precise mechanisms responsible for autoinhibition and activation are unknown due to lack of an autoinhibited MOB1 structure. Here, we report on the crystal structure of full-length MOB1B in the autoinhibited form and a complex between the MOB1B core domain and the N-terminal regulation (NTR) domain of LATS1. The structure of full-length MOB1B shows that the N-terminal extension forms a short β-strand, the SN strand, followed by a long conformationally flexible positively-charged linker and α-helix, the Switch helix, which blocks the LATS1 binding surface of MOB1B. The Switch helix is stabilized by β-sheet formation of the SN strand with the S2 strand of the MOB1 core domain. Phosphorylation of Thr12 and Thr35 residues structurally accelerates dissociation of the Switch helix from the LATS1-binding surface by the "pull-the-string" mechanism, thereby enabling LATS1 binding.

PubMed: 27335147
DOI: 10.1038/srep28488

実験手法

X-RAY DIFFRACTION (2.957 Å)