1ncj

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(New page: 200px<br /><applet load="1ncj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ncj, resolution 3.4&Aring;" /> '''N-CADHERIN, TWO-DOMAI...)
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[[Image:1ncj.gif|left|200px]]<br /><applet load="1ncj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ncj.gif|left|200px]]<br /><applet load="1ncj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ncj, resolution 3.4&Aring;" />
caption="1ncj, resolution 3.4&Aring;" />
'''N-CADHERIN, TWO-DOMAIN FRAGMENT'''<br />
'''N-CADHERIN, TWO-DOMAIN FRAGMENT'''<br />
==Overview==
==Overview==
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To investigate the possible biological function of the lateral "strand, dimer" observed in crystal structures of a D1 domain extracellular, fragment from N-cadherin, we have undertaken site-directed mutagenesis, studies of this molecule. Mutation of most residues important in the, strand dimer interface abolish the ability of N-cadherin to mediate cell, adhesion. Mutation of an analogous central residue (Trp-2) in E-cadherin, also abrogates the adhesive capacity of that molecule. We also determined, the crystal structure of a Ca2+-complexed two-domain fragment from, N-cadherin. This structure, like its E-cadherin counterpart, does not, adopt the strand dimer conformation. This suggests the possibility that, classical cadherins might stably exist in both dimeric and monomeric, forms. Data from several laboratories imply that lateral dimerization or, clustering of cadherins may increase their adhesivity. We suggest the, possibility that the strand dimer may play a role in this activation.
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To investigate the possible biological function of the lateral "strand dimer" observed in crystal structures of a D1 domain extracellular fragment from N-cadherin, we have undertaken site-directed mutagenesis studies of this molecule. Mutation of most residues important in the strand dimer interface abolish the ability of N-cadherin to mediate cell adhesion. Mutation of an analogous central residue (Trp-2) in E-cadherin also abrogates the adhesive capacity of that molecule. We also determined the crystal structure of a Ca2+-complexed two-domain fragment from N-cadherin. This structure, like its E-cadherin counterpart, does not adopt the strand dimer conformation. This suggests the possibility that classical cadherins might stably exist in both dimeric and monomeric forms. Data from several laboratories imply that lateral dimerization or clustering of cadherins may increase their adhesivity. We suggest the possibility that the strand dimer may play a role in this activation.
==About this Structure==
==About this Structure==
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1NCJ 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 and IUM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NCJ OCA].
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1NCJ 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> and <scene name='pdbligand=IUM:'>IUM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NCJ OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Colman, D.R.]]
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[[Category: Colman, D R.]]
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[[Category: Hendrickson, W.A.]]
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[[Category: Hendrickson, W A.]]
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[[Category: Shan, W.S.]]
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[[Category: Shan, W S.]]
[[Category: Shapiro, L.]]
[[Category: Shapiro, L.]]
[[Category: Tamura, K.]]
[[Category: Tamura, K.]]
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[[Category: cell adhesion protein]]
[[Category: cell adhesion protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:08:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:36 2008''

Revision as of 12:04, 21 February 2008


1ncj, resolution 3.4Å

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N-CADHERIN, TWO-DOMAIN FRAGMENT

Overview

To investigate the possible biological function of the lateral "strand dimer" observed in crystal structures of a D1 domain extracellular fragment from N-cadherin, we have undertaken site-directed mutagenesis studies of this molecule. Mutation of most residues important in the strand dimer interface abolish the ability of N-cadherin to mediate cell adhesion. Mutation of an analogous central residue (Trp-2) in E-cadherin also abrogates the adhesive capacity of that molecule. We also determined the crystal structure of a Ca2+-complexed two-domain fragment from N-cadherin. This structure, like its E-cadherin counterpart, does not adopt the strand dimer conformation. This suggests the possibility that classical cadherins might stably exist in both dimeric and monomeric forms. Data from several laboratories imply that lateral dimerization or clustering of cadherins may increase their adhesivity. We suggest the possibility that the strand dimer may play a role in this activation.

About this Structure

1NCJ is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure-function analysis of cell adhesion by neural (N-) cadherin., Tamura K, Shan WS, Hendrickson WA, Colman DR, Shapiro L, Neuron. 1998 Jun;20(6):1153-63. PMID:9655503

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