5DZZ

Structural characterization of intermediate filaments binding domain of desmoplakin

Summary for 5DZZ

• Entry DOI: 10.2210/pdb5dzz/pdb
• Descriptor: Desmoplakin (2 entities in total)
• Functional Keywords: desmoplakin, prd, intermediate filaments, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 54555.17

Authors

Choi, H.-J.,Weis, W.I. (deposition date: 2015-09-26, release date: 2016-03-23, Last modification date: 2023-11-08)

Primary citation

Kang, H.,Weiss, T.M.,Bang, I.,Weis, W.I.,Choi, H.J.
Structure of the Intermediate Filament-Binding Region of Desmoplakin.
Plos One, 11:e0147641-e0147641, 2016

PubMed Abstract: Desmoplakin (DP) is a cytoskeletal linker protein that connects the desmosomal cadherin/plakoglobin/plakophilin complex to intermediate filaments (IFs). The C-terminal region of DP (DPCT) mediates IF binding, and contains three plakin repeat domains (PRDs), termed PRD-A, PRD-B and PRD-C. Previous crystal structures of PRDs B and C revealed that each is formed by 4.5 copies of a plakin repeat (PR) and has a conserved positively charged groove on its surface. Although PRDs A and B are linked by just four amino acids, B and C are separated by a 154 residue flexible linker, which has hindered crystallographic analysis of the full DPCT. Here we present the crystal structure of a DPCT fragment spanning PRDs A and B, and elucidate the overall architecture of DPCT by small angle X-ray scattering (SAXS) analysis. The structure of PRD-A is similar to that of PRD-B, and the two domains are arranged in a quasi-linear arrangement, and separated by a 4 amino acid linker. Analysis of the B-C linker region using secondary structure prediction and the crystal structure of a homologous linker from the cytolinker periplakin suggests that the N-terminal ~100 amino acids of the linker form two PR-like motifs. SAXS analysis of DPCT indicates an elongated but non-linear shape with Rg = 51.5 Å and Dmax = 178 Å. These data provide the first structural insights into an IF binding protein containing multiple PRDs and provide a foundation for studying the molecular basis of DP-IF interactions.

PubMed: 26808545
DOI: 10.1371/journal.pone.0147641

Experimental method

X-RAY DIFFRACTION (2.6 Å)