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
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Armadillo Domain Proteins
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Catenins
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / metabolism
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Crystallography, X-Ray
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Delta Catenin
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Desmosomes / chemistry
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Desmosomes / metabolism
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Humans
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Ligands
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Models, Molecular
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Molecular Sequence Data
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Phosphoproteins / chemistry
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Phosphoproteins / metabolism
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Plakophilins
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / metabolism*
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Sequence Alignment
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Static Electricity
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Structural Homology, Protein
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Trans-Activators / chemistry*
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Trans-Activators / metabolism*
Substances
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Armadillo Domain Proteins
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Catenins
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Cell Adhesion Molecules
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Ligands
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PKP1 protein, human
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Phosphoproteins
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Plakophilins
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Proteins
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Trans-Activators
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Delta Catenin
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CTNND1 protein, human