Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway

Hwang, E.; Cheong, H.-K.; Mushtaq, A.U.; Kim, H.-Y.; Yeo, K.J.; Kim, E.; Lee, W.C.; Hwang, K.Y.; Cheong, C.; Jeon, Y.H.

doi:10.1107/S139900471400947X

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
Schematic model showing how the MST1 kinase domain gains motional freedom by heterodimerization with RASSF5 in the membrane environment. The MST1 SARAH promoter undergoes structural change when it binds to the RASSF5 SARAH domain to form a heterodimer. By extension of the h2 helix and unfolding of the h1 helix, the MST1 SARAH domain in the heterodimer can provide motional freedom to the MST1 catalytic domain. The grey ribbon represents the MST1 SARAH domain in the homodimer and the blue ribbon denotes the MST1 SARAH domain in the heterodimer with RASSF5. The magenta ribbon represents the RASSF5 SARAH domain in the heterodimer with MST1. The blue horizontal bar represents a cellular membrane where the prenylated Ras protein anchors.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 70| Part 7| July 2014| Pages 1944-1953

https://doi.org/10.1107/S139900471400947X

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