1L3W
C-cadherin Ectodomain
Summary for 1L3W
| Entry DOI | 10.2210/pdb1l3w/pdb |
| Related | 1EDH 1FF5 1NCG 1NCH 1NCI |
| Descriptor | EP-cadherin, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | cell adhesion, calcium binding, cadherin, extracellular, ectodomain, metal binding protein |
| Biological source | Xenopus laevis (African clawed frog) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P33148 |
| Total number of polymer chains | 1 |
| Total formula weight | 64205.15 |
| Authors | Boggon, T.J.,Murray, J.,Chappuis-Flament, S.,Wong, E.,Gumbiner, B.M.,Shapiro, L. (deposition date: 2002-03-01, release date: 2002-04-26, Last modification date: 2023-08-16) |
| Primary citation | Boggon, T.J.,Murray, J.,Chappuis-Flament, S.,Wong, E.,Gumbiner, B.M.,Shapiro, L. C-cadherin ectodomain structure and implications for cell adhesion mechanisms Science, 296:1308-1313, 2002 Cited by PubMed Abstract: 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. PubMed: 11964443DOI: 10.1126/science.1071559 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.08 Å) |
Structure validation
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