PDBsum entry 1suh

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Cell adhesion PDB id
Protein chain
104 a.a. *
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Amino-terminal domain of epithelial cadherin in the calcium bound state, nmr, 20 structures
Structure: Epithelial cadherin. Chain: a. Fragment: amino-terminal domain residues 1 - 104. Synonym: uvomorulin. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Tissue: epithelial, neural. Gene: x06115 (genbank). Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: M.Overduin,K.I.Tong,C.M.Kay,M.Ikura
Key ref: M.Overduin et al. (1996). 1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin. J Biomol NMR, 7, 173-189. PubMed id: 8785495
30-Jan-96     Release date:   11-Jul-96    
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Protein chain
Pfam   ArchSchema ?
P09803  (CADH1_MOUSE) -  Cadherin-1
884 a.a.
104 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   3 terms 
  Biological process     cell adhesion   3 terms 
  Biochemical function     calcium ion binding     1 term  


J Biomol NMR 7:173-189 (1996)
PubMed id: 8785495  
1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin.
M.Overduin, K.I.Tong, C.M.Kay, M.Ikura.
E-cadherin is a transmembrane protein that provides Ca(2+)-dependent cell adhesion to epithelial cells. The large majority of the 1H, 15N, 13C and 13CO resonances of a 146-amino acid polypeptide from epithelial (E-) cadherin have been assigned using multidimensional NMR spectroscopy. The structure of the amino-terminal 100 amino acids, corresponding to the first extracellular repeat of E-cadherin [Overduin et al. (1995) Science, 267, 386-389], has been refined. The monomeric state of this isolated domain is demonstrated by light scattering and sedimentation analysis. Seven beta-strands and two short helices were identified by patterns of NOE cross-peaks, vicinal coupling constants and chemical shift indices. A novel structural motif termed a quasi-beta-helix found in the crystal structure of a neural (N-) cadherin domain [Shapiro et al. (1995) Nature, 374, 327-337] is characterized in detail for the first time by NMR. Slowly exchanging amides were concentrated in the beta-sheet region and quasi-beta-helix. The beta-barrel fold of the cadherin domain is topologically similar to the immunoglobulin fold. Comparison of this solution structure to the crystallized dimers of the N-terminal pair of E-cadherin domains [Nagar et al. (1996) Nature, 380, 360-364] and of the homologous single domain of N-cadherin reveals a conserved cadherin fold with minor structural differences, which can be accounted for by differences in metal ligation and oligomeric state.

Literature references that cite this PDB file's key reference

  PubMed id Reference
16287100 A.Prasad, H.Zhao, J.M.Rutherford, N.Housley, C.Nichols, and S.Pedigo (2006).
Effect of linker segments on the stability of epithelial cadherin Domain 2.
  Proteins, 62, 111-121.  
16183887 F.Cailliez, and R.Lavery (2005).
Cadherin mechanics and complexation: the importance of calcium binding.
  Biophys J, 89, 3895-3903.  
15112230 J.M.Gooding, K.L.Yap, and M.Ikura (2004).
The cadherin-catenin complex as a focal point of cell adhesion and signalling: new insights from three-dimensional structures.
  Bioessays, 26, 497-511.  
11856755 I.T.Makagiansar, P.D.Nguyen, A.Ikesue, K.Kuczera, W.Dentler, J.L.Urbauer, N.Galeva, M.Alterman, and T.J.Siahaan (2002).
Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat.
  J Biol Chem, 277, 16002-16010.  
11821414 S.Bibert, M.Jaquinod, E.Concord, C.Ebel, E.Hewat, C.Vanbelle, P.Legrand, M.Weidenhaupt, T.Vernet, and D.Gulino-Debrac (2002).
Synergy between extracellular modules of vascular endothelial cadherin promotes homotypic hexameric interactions.
  J Biol Chem, 277, 12790-12801.  
10727102 W.Yang, T.Tsai, M.Kats, and J.J.Yang (2000).
Peptide analogs from E-cadherin with different calcium-binding affinities.
  J Pept Res, 55, 203-215.  
10394369 T.G.Kutateladze, K.D.Ogburn, W.T.Watson, Beer, S.D.Emr, C.G.Burd, and M.Overduin (1999).
Phosphatidylinositol 3-phosphate recognition by the FYVE domain.
  Mol Cell, 3, 805-811.  
9655503 K.Tamura, W.S.Shan, W.A.Hendrickson, D.R.Colman, and L.Shapiro (1998).
Structure-function analysis of cell adhesion by neural (N-) cadherin.
  Neuron, 20, 1153-1163.
PDB code: 1ncj
9721102 Beer, R.E.Carter, K.E.Lobel-Rice, A.Sorkin, and M.Overduin (1998).
Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.
  Science, 281, 1357-1360.
PDB code: 1eh2
9442878 D.J.Leahy (1997).
Implications of atomic-resolution structures for cell adhesion.
  Annu Rev Cell Dev Biol, 13, 363-393.  
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