Purification and Structural Analysis of Desmoplakin
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Updated: Mar 27, 2026

Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
Published on: October 15, 2019
Hee-Jung Choi1, William I Weis2
1School of Biological Sciences, Seoul National University, Seoul, South Korea.
Abstract:
Desmoplakin (DP) is an obligate component of desmosomes, where it links the desmosomal cadherin/plakoglobin/plakophilin assembly to intermediate filaments. DP contains a large amino-terminal domain (DPNT) that binds to the cadherin/plakoglobin/plakophilin complex, a central coiled-coil domain that dimerizes the molecule, and a C-terminal domain (DPCT) that binds to intermediate filaments. DPNT contains a plakin domain, comprising a set of spectrin-like repeats. DPCT contains three plakin repeat domains, each formed by 4.5 repeats of a sequence motif known as a plakin repeat that bind to intermediate filaments. Here, we review purification, biochemical characterization, and structural analysis of the DPNT plakin domain and the DPCT plakin repeat domains.
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