|
|
| Line 1: |
Line 1: |
| [[Image:1suh.gif|left|200px]] | | {{Seed}} |
| | [[Image:1suh.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1suh| PDB=1suh | SCENE= }} | | {{STRUCTURE_1suh| PDB=1suh | SCENE= }} |
|
| |
|
| '''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=== |
|
| |
|
|
| |
|
| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8785495}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8785495 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_8785495}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| 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]. | | 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== |
| Line 29: |
Line 33: |
| [[Category: Calcium binding]] | | [[Category: Calcium binding]] |
| [[Category: Cell adhesion]] | | [[Category: Cell adhesion]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:08:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:08:43 2008'' |