1q1p: Difference between revisions
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|PDB= 1q1p |SIZE=350|CAPTION= <scene name='initialview01'>1q1p</scene>, resolution 3.20Å | |PDB= 1q1p |SIZE=350|CAPTION= <scene name='initialview01'>1q1p</scene>, resolution 3.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CDH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= CDH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ff5|1FF5]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1p OCA], [http://www.ebi.ac.uk/pdbsum/1q1p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q1p RCSB]</span> | |||
}} | }} | ||
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[[Category: Haussinger, D.]] | [[Category: Haussinger, D.]] | ||
[[Category: Stetefeld, J.]] | [[Category: Stetefeld, J.]] | ||
[[Category: cell-adhesion]] | [[Category: cell-adhesion]] | ||
''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 23:07:35 2008'' | ||
Revision as of 20:07, 30 March 2008
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| 1q1p, resolution 3.20Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CA | ||||||||||||
| Gene: | CDH1 (Mus musculus) | ||||||||||||
| Related: | 1FF5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
E-Cadherin activation
Overview
Cellular adhesion by classical cadherins depends critically on the exact proteolytic removal of their N-terminal prosequences. In this combined solution NMR and X-ray crystallographic study, the consequences of propeptide cleavage of an epithelial cadherin construct (domains 1 and 2) were followed at atomic level. At low protein concentration, the N-terminal processing induces docking of the tryptophan-2 side-chain into a binding pocket on the same molecule. At high concentration, cleavage induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1)) and concomitant intermolecular exchange of the betaA-strands and the tryptophan-2 side-chains. Thus, the cleavage represents the switch from a nonadhesive to the functional form of cadherin.
About this Structure
1Q1P is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography., Haussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S, EMBO J. 2004 Apr 21;23(8):1699-708. Epub 2004 Apr 8. PMID:15071499
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