Fig. 4: Analysis of the interactions between TRIP12 and triUbK29/K48. | Nature Communications

Fig. 4: Analysis of the interactions between TRIP12 and triUbK29/K48.

From: Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination

Fig. 4: Analysis of the interactions between TRIP12 and triUbK29/K48.

a Cryo-EM density (a) and structural model (b) of the TRIP12-triUbK29/K48 complex. c Structural alignment of Ufd4-triUbK29/K48 complex and TRIP12-triUbK29/K48 complex structures, and only ARM region, C-lobe and K48-linked diUb are shown. d, e Molecular interactions between the ARM region and UbK48−dist (d), the ARM region and UbK48−prox (e). f–h Molecular interactions between the C-lobe and UbK48−prox.

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