1edh: Difference between revisions

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[[Image:1edh.gif|left|200px]]
[[Image:1edh.gif|left|200px]]


{{Structure
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|DOMAIN=
{{STRUCTURE_1edh| PDB=1edh  | SCENE= }}  
|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>
}}


'''E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM'''
'''E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM'''
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[[Category: Overduin, M.]]
[[Category: Overduin, M.]]
[[Category: Rini, J M.]]
[[Category: Rini, J M.]]
[[Category: cadherin]]
[[Category: Cadherin]]
[[Category: calcium binding protein]]
[[Category: Calcium binding protein]]
[[Category: cell adhesion protein]]
[[Category: Cell adhesion protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:22 2008''

Revision as of 14:57, 2 May 2008

File:1edh.gif

Template:STRUCTURE 1edh

E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM


OverviewOverview

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 StructureAbout this Structure

1EDH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

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