3K6F

Crystal structure of mouse T-cadherin EC1

Summary for 3K6F

• Entry DOI: 10.2210/pdb3k6f/pdb
• Related: 3K6D 3K6I
• Descriptor: T-cadherin (2 entities in total)
• Functional Keywords: t-cadherin, cell adhesion, calcium, cell membrane, cleavage on pair of basic residues, glycoprotein, gpi-anchor, lipoprotein, membrane
• Biological source: Mus musculus (mouse)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor (By similarity): Q9WTR5
• Total number of polymer chains: 2
• Total formula weight: 21850.41

Authors

Shapiro, L.,Ciatto, C. (deposition date: 2009-10-08, release date: 2010-03-02, Last modification date: 2023-09-06)

Primary citation

Ciatto, C.,Bahna, F.,Zampieri, N.,Vansteenhouse, H.C.,Katsamba, P.S.,Ahlsen, G.,Harrison, O.J.,Brasch, J.,Jin, X.,Posy, S.,Vendome, J.,Ranscht, B.,Jessell, T.M.,Honig, B.,Shapiro, L.
T-cadherin structures reveal a novel adhesive binding mechanism
Nat.Struct.Mol.Biol., 17:339-347, 2010

PubMed Abstract: Vertebrate genomes encode 19 classical cadherins and about 100 nonclassical cadherins. Adhesion by classical cadherins depends on binding interactions in their N-terminal EC1 domains, which swap N-terminal beta-strands between partner molecules from apposing cells. However, strand-swapping sequence signatures are absent from nonclassical cadherins, raising the question of how these proteins function in adhesion. Here, we show that T-cadherin, a glycosylphosphatidylinositol (GPI)-anchored cadherin, forms dimers through an alternative nonswapped interface near the EC1-EC2 calcium-binding sites. Mutations within this interface ablate the adhesive capacity of T-cadherin. These nonadhesive T-cadherin mutants also lose the ability to regulate neurite outgrowth from T-cadherin-expressing neurons. Our findings reveal the likely molecular architecture of the T-cadherin homophilic interface and its requirement for axon outgrowth regulation. The adhesive binding mode used by T-cadherin may also be used by other nonclassical cadherins.

PubMed: 20190755
DOI: 10.1038/nsmb.1781

Experimental method

X-RAY DIFFRACTION (1.813 Å)