1q1p
From Proteopedia
(New page: 200px<br /><applet load="1q1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q1p, resolution 3.20Å" /> '''E-Cadherin activatio...) |
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| - | [[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size=" | + | [[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q1p, resolution 3.20Å" /> | caption="1q1p, resolution 3.20Å" /> | ||
'''E-Cadherin activation'''<br /> | '''E-Cadherin activation'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cellular adhesion by classical cadherins depends critically on the exact | + | 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== | ==About this Structure== | ||
| - | 1Q1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Q1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: cell-adhesion]] | [[Category: cell-adhesion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:55 2008'' |
Revision as of 12:34, 21 February 2008
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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 with as ligand. 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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