Structure of the armadillo repeat domain of plakophilin 1

J Mol Biol. 2005 Feb 11;346(1):367-76. doi: 10.1016/j.jmb.2004.11.048. Epub 2004 Dec 19.

Abstract

The p120ctn subfamily of armadillo domain proteins has roles in modulating intercellular adhesion by cadherin-containing junctions. We have determined the crystal structure of the arm repeat domain from plakophilin-1 (PKP1), a member of the p120ctn subfamily that is found in desmosomes. The structure reveals that the domain has nine instead of the expected ten arm repeats. A sequence predicted to be an arm repeat is instead a large insert which serves as a wedge that produces a significant bend in the overall domain structure. Structure-based sequence alignments indicate that the nine repeats and large insert are common to this subfamily of armadillo proteins. A prominent basic patch on the surface of the protein may serve as a binding site for partners of these proteins.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Armadillo Domain Proteins
  • Catenins
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism
  • Crystallography, X-Ray
  • Desmosomes / chemistry
  • Desmosomes / metabolism
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Plakophilins
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Sequence Alignment
  • Static Electricity
  • Structural Homology, Protein
  • Trans-Activators / chemistry*
  • Trans-Activators / metabolism*

Substances

  • Armadillo Domain Proteins
  • Catenins
  • Cell Adhesion Molecules
  • Ligands
  • PKP1 protein, human
  • Phosphoproteins
  • Plakophilins
  • Proteins
  • Trans-Activators
  • delta catenin