1ncj
From Proteopedia
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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 CA and IUM 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
Page seeded by OCA on Tue Nov 20 22:08:17 2007
