This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1edh
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1edh.gif|left|200px]] | [[Image:1edh.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1edh", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1edh| PDB=1edh | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM''' | '''E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM''' | ||
| Line 29: | Line 26: | ||
[[Category: Overduin, M.]] | [[Category: Overduin, M.]] | ||
[[Category: Rini, J M.]] | [[Category: Rini, J M.]] | ||
| - | [[Category: | + | [[Category: Cadherin]] |
| - | [[Category: | + | [[Category: Calcium binding protein]] |
| - | [[Category: | + | [[Category: Cell adhesion protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:57:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:57, 2 May 2008
E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM
Overview
The cadherins mediate cell adhesion and play a fundamental role in normal development. They participate in the maintenance of proper cell-cell contacts: for example, reduced levels of epithelial cadherin (E-cadherin) correlate with increased invasiveness in many human tumour cell types. The cadherins typically consist of five tandemly repeated extracellular domains, a single membrane-spanning segment and a cytoplasmic region. The N-terminal extracellular domains mediate cell-cell contact while the cytoplasmic region interacts with the cytoskeleton through the catenins. Cadherins depend on calcium for their function: removal of calcium abolishes adhesive activity, renders cadherins vulnerable to proteases (reviewed in ref. 4) and, in E-cadherin, induces a dramatic reversible conformational change in the entire extracellular region. We report here the X-ray crystal structure at 2.0 A resolution of the two N-terminal extracellular domains of E-cadherin in the presence of calcium. The structure reveals a two-fold symmetric dimer, each molecule of which binds a contiguous array of three bridged calcium ions. Not only do the bound calcium ions linearize and rigidify the molecule, they promote dimerization. Although the N-terminal domain of each molecule in the dimer is aligned in a parallel orientation, the interactions between them differ significantly from those found in the neural cadherin (N-cadherin) N-terminal domain (NCD1) structure. The E-cadherin dual-domain structure reported here defines the role played by calcium in the cadherin-mediated formation and maintenance of solid tissues.
About this Structure
1EDH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of calcium-induced E-cadherin rigidification and dimerization., Nagar B, Overduin M, Ikura M, Rini JM, Nature. 1996 Mar 28;380(6572):360-4. PMID:8598933 Page seeded by OCA on Fri May 2 14:57:51 2008
