THE CONFORMATION OF CLATHRIN LIGHT-CHAINS ON TRISKELIONS PROBED BY ANTIBODY INHIBITION

The conformation of clathrin light-chains along the proximal arm of th e clathrin triskelion was studied by using rabbit anti-(light-chain pe ptides) to inhibit the binding of a mouse monoclonal antibody against an epitope in the amino-terminal region. Prior incubation of triskelio ns with rabbit antisera raised against the extreme carboxyl-terminal o f the light-chains partially inhibited binding. The inhibition was lar gely removed when tested on light-chains that had been freed from tris kelions. This suggests that when the light-chains bind the heavy-chain , they adopt a conformation in which the amino and carboxyl-terminal d omains are not fully extended, but fold such that these two domains fa ce each other. (C) 1996 Academic Press Limited