1q1p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1q1p.gif|left|200px]]
[[Image:1q1p.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1q1p |SIZE=350|CAPTION= <scene name='initialview01'>1q1p</scene>, resolution 3.20&Aring;
+
The line below this paragraph, containing "STRUCTURE_1q1p", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= CDH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1q1p| PDB=1q1p | SCENE= }}
-
|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>
+
-
}}
+
'''E-Cadherin activation'''
'''E-Cadherin activation'''
Line 27: Line 24:
[[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 Sat May 3 05:45:31 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:35 2008''
+

Revision as of 02:45, 3 May 2008

Image:1q1p.gif

Template:STRUCTURE 1q1p

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 Page seeded by OCA on Sat May 3 05:45:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q1p"
Personal tools