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 4
Comparison of the urea-induced denaturation curves of SARAH domains. The secondary-structural changes in the SARAH domains upon increases in the urea concentration were observed by monitoring the molar ellipticity [θ] at 222 nm in far-UV circular dichroism (CD) for the MST1–RASSF5 SARAH heterodimer (a), the MST1 SARAH homodimer (b), the MST2–RASSF5 SARAH heterodimer (c), the MST2 SARAH homodimer (d) and a double-mutant MST1–RASSF5 (E388A and K398A of RASSF5) SARAH heterodimer (e). Dotted lines indicate the transition concentration (C_m) of urea for the denaturation of α-helical structures.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S139900471400947X

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