1ff5: Difference between revisions

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[[Image:1ff5.gif|left|200px]]
[[Image:1ff5.gif|left|200px]]


{{Structure
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|PDB= 1ff5 |SIZE=350|CAPTION= <scene name='initialview01'>1ff5</scene>, resolution 2.93&Aring;
The line below this paragraph, containing "STRUCTURE_1ff5", creates the "Structure Box" on the page.
|SITE=
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|DOMAIN=
{{STRUCTURE_1ff5|  PDB=1ff5 |  SCENE= }}  
|RELATEDENTRY=[[1edh|1EDH]], [[1ncj|1NCJ]], [[1ncg|1NCG]], [[1nch|1NCH]], [[1shu|1SHU]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ff5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ff5 OCA], [http://www.ebi.ac.uk/pdbsum/1ff5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ff5 RCSB]</span>
}}


'''STRUCTURE OF E-CADHERIN DOUBLE DOMAIN'''
'''STRUCTURE OF E-CADHERIN DOUBLE DOMAIN'''
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[[Category: Koch, A W.]]
[[Category: Koch, A W.]]
[[Category: Pertz, O.]]
[[Category: Pertz, O.]]
[[Category: ca-binding]]
[[Category: Ca-binding]]
[[Category: e-cadherin]]
[[Category: E-cadherin]]
 
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Revision as of 16:15, 2 May 2008

File:1ff5.gif

Template:STRUCTURE 1ff5

STRUCTURE OF E-CADHERIN DOUBLE DOMAIN


OverviewOverview

Electron microscopy of ECADCOMP, a recombinant E-cadherin ectodomain pentamerized by the assembly domain of cartilage oligomeric matrix protein, has been used to analyze the role of cis-dimerization and trans-interaction in the homophilic association of this cell adhesion molecule. The Ca2+ dependency of both interactions was investigated. Low Ca2+ concentrations (50 microM) stabilized the rod-like structure of E-cadherin. At medium Ca2+ concentration (500 microM), two adjacent ectodomains in a pentamer formed cis-dimers. At high Ca2+ concentration (>1 mM), two cis-dimers from different pentamers formed a trans-interaction. The X-ray structure of an N-terminal domain pair of E-cadherin revealed two molecules per asymmetric unit in an intertwisted X-shaped arrangement with closest contacts in the Ca2+-binding region between domains 1 and 2. Contrary to previous data, Trp2 was docked in the hydrophobic cavity of its own molecule, and was therefore not involved in cis-dimerization of two molecules. This was supported further by W2A and A80I (a residue involved in the hydrophobic cavity surrounding Trp2) mutations in ECADCOMP which both led to abrogation of the trans- but not the cis-interaction. Structural and biochemical data suggest a link between Ca2+ binding in the millimolar range and Trp2 docking, both events being essential for the trans-association.

About this StructureAbout this Structure

1FF5 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation., Pertz O, Bozic D, Koch AW, Fauser C, Brancaccio A, Engel J, EMBO J. 1999 Apr 1;18(7):1738-47. PMID:10202138 Page seeded by OCA on Fri May 2 16:15:10 2008

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