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1suh

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[[Image:1suh.gif|left|200px]]
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{{STRUCTURE_1suh| PDB=1suh | SCENE= }}
{{STRUCTURE_1suh| PDB=1suh | SCENE= }}
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'''AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES'''
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===AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_8785495}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8785495 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8785495}}
==About this Structure==
==About this Structure==
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1SUH is a [[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].
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1SUH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUH OCA].
==Reference==
==Reference==
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[[Category: Calcium binding]]
[[Category: Calcium binding]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:08:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:08:43 2008''

Revision as of 02:08, 29 July 2008

Image:1suh.png

Template:STRUCTURE 1suh

AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 8785495

About this Structure

1SUH is a Single protein structure of sequence from Mus musculus. Full experimental 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

Page seeded by OCA on Tue Jul 29 05:08:43 2008

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