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Cell adhesion PDB id
1xm9
Jmol
Contents
Protein chain
420 a.a. *
* Residue conservation analysis
PDB id:
1xm9
Name: Cell adhesion
Title: Structure of the armadillo repeat domain of plakophilin 1
Structure: Plakophilin 1. Chain: a. Fragment: armadillo repeat domain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pkp1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
2.80Å     R-factor:   0.255     R-free:   0.324
Authors: H.J.Choi,W.I.Weis
Key ref:
H.J.Choi and W.I.Weis (2005). Structure of the armadillo repeat domain of plakophilin 1. J Mol Biol, 346, 367-376. PubMed id: 15663951 DOI: 10.1016/j.jmb.2004.11.048
Date:
01-Oct-04     Release date:   22-Mar-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13835  (PKP1_HUMAN) -  Plakophilin-1
Seq:
Struc:
 
Seq:
Struc:
747 a.a.
420 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     binding     1 term  

 

 
DOI no: 10.1016/j.jmb.2004.11.048 J Mol Biol 346:367-376 (2005)
PubMed id: 15663951  
 
 
Structure of the armadillo repeat domain of plakophilin 1.
H.J.Choi, W.I.Weis.
 
  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.
 
  Selected figure(s)  
 
Figure 5.
Figure 5. Comparison of repeat motif structures. (a) A comparison of PKP1 R3 with b-catenin R3. The backbones are overlaid on the left. The individual repeats are shown on the right, with the side-chains of the conserved consensus residues shown in ball-and-stick representation. (b) A comparison of PKP1 arm repeat 3 with importin-b HEAT repeat 3.
Figure 6.
Figure 6. The effect of the H1-H2 turn on arm repeat structure. Comparison of PKP1 repeat 4, which does not contain the glycine residue found frequently in the H1-H2 turn, with b-catenin repeat 3, which has this glycine residue.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 346, 367-376) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21464301 A.Al-Amoudi, D.Castaño-Diez, D.P.Devos, R.B.Russell, G.T.Johnson, and A.S.Frangakis (2011).
The three-dimensional molecular structure of the desmosomal plaque.
  Proc Natl Acad Sci U S A, 108, 6480-6485.  
20626351 H.A.Thomason, A.Scothern, S.McHarg, and D.R.Garrod (2010).
Desmosomes: adhesive strength and signalling in health and disease.
  Biochem J, 429, 419-433.  
20371349 N.Ishiyama, S.H.Lee, S.Liu, G.Y.Li, M.J.Smith, L.F.Reichardt, and M.Ikura (2010).
Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion.
  Cell, 141, 117-128.
PDB codes: 3l6x 3l6y
20164302 P.D.McCrea, and D.Gu (2010).
The catenin family at a glance.
  J Cell Sci, 123, 637-642.  
20585595 S.Neuber, M.Mühmer, D.Wratten, P.J.Koch, R.Moll, and A.Schmidt (2010).
The desmosomal plaque proteins of the plakophilin family.
  Dermatol Res Pract, 2010, 101452.  
19674883 A.E.Bass-Zubek, L.M.Godsel, M.Delmar, and K.J.Green (2009).
Plakophilins: multifunctional scaffolds for adhesion and signaling.
  Curr Opin Cell Biol, 21, 708-716.  
19843587 D.Gu, A.K.Sater, H.Ji, K.Cho, M.Clark, S.A.Stratton, M.C.Barton, Q.Lu, and P.D.McCrea (2009).
Xenopus delta-catenin is essential in early embryogenesis and is functionally linked to cadherins and small GTPases.
  J Cell Sci, 122, 4049-4061.  
  20066089 E.Delva, D.K.Tucker, and A.P.Kowalczyk (2009).
The desmosome.
  Cold Spring Harbor Perspect Biol, 1, a002543.  
  20066110 L.Shapiro, and W.I.Weis (2009).
Structure and biochemistry of cadherins and catenins.
  Cold Spring Harbor Perspect Biol, 1, a003053.  
18496566 D.Acehan, C.Petzold, I.Gumper, D.D.Sabatini, E.J.Müller, P.Cowin, and D.L.Stokes (2008).
Plakoglobin is required for effective intermediate filament anchorage to desmosomes.
  J Invest Dermatol, 128, 2665-2675.  
18682726 S.E.Grosskurth, D.Bhattacharya, Q.Wang, and J.J.Lin (2008).
Emergence of Xin demarcates a key innovation in heart evolution.
  PLoS ONE, 3, e2857.  
17945476 D.L.Stokes (2007).
Desmosomes from a structural perspective.
  Curr Opin Cell Biol, 19, 565-571.  
18007692 J.E.Lai-Cheong, K.Arita, and J.A.McGrath (2007).
Genetic diseases of junctions.
  J Invest Dermatol, 127, 2713-2725.  
17531221 J.Uitto, G.Richard, and J.A.McGrath (2007).
Diseases of epidermal keratins and their linker proteins.
  Exp Cell Res, 313, 1995-2009.  
17934502 K.J.Green, and C.L.Simpson (2007).
Desmosomes: new perspectives on a classic.
  J Invest Dermatol, 127, 2499-2515.  
17539752 S.Pokutta, and W.I.Weis (2007).
Structure and mechanism of cadherins and catenins in cell-cell contacts.
  Annu Rev Cell Dev Biol, 23, 237-261.  
16197419 J.A.McGrath (2005).
Inherited disorders of desmosomes.
  Australas J Dermatol, 46, 221-229.  
15988759 J.K.Wahl (2005).
A role for plakophilin-1 in the initiation of desmosome assembly.
  J Cell Biochem, 96, 390-403.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.