1l3w
From Proteopedia
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- | [[Image:1l3w.gif|left|200px]] | + | [[Image:1l3w.gif|left|200px]] |
- | + | ||
- | '''C-cadherin Ectodomain''' | + | {{Structure |
+ | |PDB= 1l3w |SIZE=350|CAPTION= <scene name='initialview01'>1l3w</scene>, resolution 3.08Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''C-cadherin Ectodomain''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1L3W is a [ | + | 1L3W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3W OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11964443 11964443] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: extracellular]] | [[Category: extracellular]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:59 2008'' |
Revision as of 10:26, 20 March 2008
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, resolution 3.08Å | |||||||
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Ligands: | , and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
Page seeded by OCA on Thu Mar 20 12:25:59 2008
Categories: Single protein | Xenopus laevis | Boggon, T J. | Chappuis-Flament, S. | Gumbiner, B M. | Murray, J. | Shapiro, L. | Wong, E. | CA | NAG | NDG | Cadherin | Calcium binding | Cell adhesion | Ectodomain | Extracellular