1edh
From Proteopedia
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|PDB= 1edh |SIZE=350|CAPTION= <scene name='initialview01'>1edh</scene>, resolution 2.0Å | |PDB= 1edh |SIZE=350|CAPTION= <scene name='initialview01'>1edh</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edh OCA], [http://www.ebi.ac.uk/pdbsum/1edh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1edh RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Overduin, M.]] | [[Category: Overduin, M.]] | ||
[[Category: Rini, J M.]] | [[Category: Rini, J M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HG]] | ||
[[Category: cadherin]] | [[Category: cadherin]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
[[Category: cell adhesion protein]] | [[Category: cell adhesion protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:22 2008'' |
Revision as of 17:00, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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