PDBsum entry 5dzz

Structural protein

PDB id: 5dzz

Contents

Protein chain

489 a.a.

Waters ×84

PDB id:

5dzz

Name:

Structural protein

Title:

Structural characterization of intermediate filaments binding domain of desmoplakin

Structure:

Desmoplakin. Chain: a. Fragment: unp residues 1960-2448. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dsp. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.60Å R-factor: 0.212 R-free: 0.264

Authors:

H.-J.Choi,W.I.Weis

Key ref:

H.Kang et al. (2016). Structure of the Intermediate Filament-Binding Region of Desmoplakin. Plos One, 11, e0147641. PubMed id: 26808545 DOI: 10.1371/journal.pone.0147641

Date:

26-Sep-15 Release date: 23-Mar-16

Protein chain

P15924  (DESP_HUMAN) -  Desmoplakin from Homo sapiens

Seq: 2871 a.a.

Struc: 489 a.a.

DOI no: 10.1371/journal.pone.0147641

Plos One 11:e0147641 (2016)

PubMed id: 26808545

Structure of the Intermediate Filament-Binding Region of Desmoplakin.

H.Kang, T.M.Weiss, I.Bang, W.I.Weis, H.J.Choi.

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.