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| | ==AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES== | | ==AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND STATE, NMR, 20 STRUCTURES== |
| - | <StructureSection load='1suh' size='340' side='right' caption='[[1suh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1suh' size='340' side='right'caption='[[1suh]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1suh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SUH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1suh]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUH FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">X06115 (GENBANK) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1suh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suh OCA], [http://pdbe.org/1suh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1suh RCSB], [http://www.ebi.ac.uk/pdbsum/1suh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1suh ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1suh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suh OCA], [https://pdbe.org/1suh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1suh RCSB], [https://www.ebi.ac.uk/pdbsum/1suh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1suh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CADH1_MOUSE CADH1_MOUSE]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity). | + | [https://www.uniprot.org/uniprot/CADH1_MOUSE CADH1_MOUSE] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Cadherin|Cadherin]] | + | *[[Cadherin 3D structures|Cadherin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Ikura, M]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kay, C M]] | + | [[Category: Ikura M]] |
| - | [[Category: Overduin, M]] | + | [[Category: Kay CM]] |
| - | [[Category: Tong, K I]] | + | [[Category: Overduin M]] |
| - | [[Category: Cadherin]] | + | [[Category: Tong KI]] |
| - | [[Category: Calcium binding]]
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| - | [[Category: Cell adhesion]]
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| Structural highlights
Function
CADH1_MOUSE Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Overduin M, Tong KI, Kay CM, Ikura M. 1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin. J Biomol NMR. 1996 May;7(3):173-89. PMID:8785495
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