PDBsum entry 1suh

Cell adhesion

PDB id

1suh

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Contents

			Protein chain

					104 a.a. *

* Residue conservation analysis

PDB id:

1suh

Links

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

Date:

30-Jan-96

Release date:

11-Jul-96

PROCHECK

	Headers

	References

Protein chain

P09803 (CADH1_MOUSE) - Cadherin-1 from Mus musculus

Seq: Struc:

Seq: Struc:					884 a.a. 104 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	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.

ABSTRACT

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, T.de 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

T.de 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.

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 code is shown on the right.