1q1p: Difference between revisions

Line 1:

[[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1q1p, resolution 3.20Å" />

'''E-Cadherin activation'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Q1P OCA].

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==

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[[Category: cell-adhesion]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 00:18:~~36 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1q1p, resolution 3.20&Aring;" />
 '''E-Cadherin activation'''<br />
 ==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.
+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==
-Q1P 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q1P OCA].
+Q1P 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==
@@ Line 18: / Line 18: @@
 [[Category: cell-adhesion]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:18:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:55 2008''