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Fig. 6. Removing Trp2 or blocking the hydrophobic acceptor pocket. (a) K562 cells expressing wild-type or mutant N-cadherin were tested for adhesion to N-cadherin Fc (1 µg/ml) bearing either the mutation Trp2Gly (W2G) or the pocket-blocking mutation Ala80Ile (A80I). The Trp2Gly mutant acted as a strand acceptor and therefore adhered to cells expressing the Glu89Ala (E89A) mutation. In contrast, the Ala80Ile mutant behaved as a strand donor because intramolecular docking of Trp2 was denied and therefore bound to cells expressing the Gly-Gly N-terminal extension mutant (GG). (b) Dynabeads coated with the Trp2Gly mutant or the Ala80Ile mutant were tested for aggregation separately or as a mixture and compared with aggregation mediated by wild-type N-cadherin. Aggregation was assessed by microscopy. The Asp134Ala (D134A) mutant served as a negative control and here, the 2.8 µm diameter beads remained monodisperse.
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