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| - | [[Image:1edh.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1edh.png|left|200px]] |
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| | {{STRUCTURE_1edh| PDB=1edh | SCENE= }} | | {{STRUCTURE_1edh| PDB=1edh | SCENE= }} |
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| - | '''E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM'''
| + | ===E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8598933}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8598933 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8598933}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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 Fri May 2 14:57:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:31:45 2008'' |
Revision as of 21:31, 30 June 2008
Template:STRUCTURE 1edh
E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM
Template:ABSTRACT PUBMED 8598933
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 Tue Jul 1 00:31:45 2008
