Structure-function analysis of cell adhesion by neural (N-) cadherin

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...

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Veröffentlicht in:	Neuron (Cambridge, Mass.) Mass.), 1998-06, Vol.20 (6), p.1153-1163
Hauptverfasser:	Tamura, K, Shan, W S, Hendrickson, W A, Colman, D R, Shapiro, L
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites - physiology Cadherins - chemistry Cadherins - genetics Cadherins - metabolism Calcium - metabolism Cell Adhesion - drug effects Cell Adhesion - physiology Cells, Cultured Crystallography Dimerization Gene Expression Image Processing, Computer-Assisted Mice Molecular Sequence Data Mutagenesis Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Protein Conformation Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Transfection Tryptophan - analogs & derivatives Tryptophan - pharmacology
Online-Zugang:	Volltext
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