1l3w

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(New page: 200px<br /><applet load="1l3w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3w, resolution 3.08&Aring;" /> '''C-cadherin Ectodomai...)
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[[Image:1l3w.gif|left|200px]]<br /><applet load="1l3w" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l3w.gif|left|200px]]<br /><applet load="1l3w" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l3w, resolution 3.08&Aring;" />
caption="1l3w, resolution 3.08&Aring;" />
'''C-cadherin Ectodomain'''<br />
'''C-cadherin Ectodomain'''<br />
==Overview==
==Overview==
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Cadherins are transmembrane proteins that mediate adhesion between cells, in the solid tissues of animals. Here we present the 3.1 angstrom, resolution crystal structure of the whole, functional extracellular domain, from C-cadherin, a representative "classical" cadherin. The structure, suggests a molecular mechanism for adhesion between cells by classical, cadherins, and it provides a new framework for understanding both cis, (same cell) and trans (juxtaposed cell) cadherin interactions. The trans, adhesive interface is a twofold symmetric interaction defined by a, conserved tryptophan side chain at the membrane-distal end of a cadherin, molecule from one cell, which inserts into a hydrophobic pocket at the, membrane-distal end of a cadherin molecule from the opposing cell.
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Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative "classical" cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.
==About this Structure==
==About this Structure==
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1L3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with NAG, NDG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L3W OCA].
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1L3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3W OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Boggon, T.J.]]
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[[Category: Boggon, T J.]]
[[Category: Chappuis-Flament, S.]]
[[Category: Chappuis-Flament, S.]]
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[[Category: Gumbiner, B.M.]]
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[[Category: Gumbiner, B M.]]
[[Category: Murray, J.]]
[[Category: Murray, J.]]
[[Category: Shapiro, L.]]
[[Category: Shapiro, L.]]
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[[Category: extracellular]]
[[Category: extracellular]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:13:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:02 2008''

Revision as of 11:41, 21 February 2008


1l3w, resolution 3.08Å

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C-cadherin Ectodomain

Overview

Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative "classical" cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.

About this Structure

1L3W is a Single protein structure of sequence from Xenopus laevis with , and as ligands. Full crystallographic information is available from OCA.

Reference

C-cadherin ectodomain structure and implications for cell adhesion mechanisms., Boggon TJ, Murray J, Chappuis-Flament S, Wong E, Gumbiner BM, Shapiro L, Science. 2002 May 17;296(5571):1308-13. Epub 2002 Apr 18. PMID:11964443

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