1suh: Difference between revisions
New page: left|200px<br /><applet load="1suh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1suh" /> '''AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN... |
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[[Image:1suh.gif|left|200px]]<br /><applet load="1suh" size=" | [[Image:1suh.gif|left|200px]]<br /><applet load="1suh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES'''<br /> | '''AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
E-cadherin is a transmembrane protein that provides Ca(2+)-dependent cell | 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== | ==About this Structure== | ||
1SUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1SUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ikura, M.]] | [[Category: Ikura, M.]] | ||
[[Category: Kay, C | [[Category: Kay, C M.]] | ||
[[Category: Overduin, M.]] | [[Category: Overduin, M.]] | ||
[[Category: Tong, K | [[Category: Tong, K I.]] | ||
[[Category: cadherin]] | [[Category: cadherin]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:17 2008'' | ||
Revision as of 13:05, 21 February 2008
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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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