1suh
From Proteopedia
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AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1SUH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin., Overduin M, Tong KI, Kay CM, Ikura M, J Biomol NMR. 1996 May;7(3):173-89. PMID:8785495
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