The conformation of clathrin light-chains on triskelions probed by antibody inhibition.
The conformation of clathrin light-chains along the proximal arm of the clathrin triskelion was studied by using rabbit anti-(light-chain peptides) to inhibit the binding of a mouse monoclonal antibody against an epitope in the amino-terminal region. Prior incubation of triskelions with rabbit antisera raised against the extreme carboxyl-terminal of the light-chains partially inhibited binding. The inhibition was largely removed when tested on light-chains that had been freed from triskelions. This suggests that when the light-chains bind the heavy-chain, they adopt a conformation in which the amino and carboxyl-terminal domains are not fully extended, but fold such that these two domains face each other.
Jackson
A P
AP
Department of Biochemistry, University of Cambridge, UK.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D001667:Binding, Competitive / Q000276:immunology; D002966:Clathrin / Q000737:chemistry* / Q000276:immunology*; D018604:Epitope Mapping; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000276:immunology; D011487:Protein Conformation; D011817:Rabbits; D013552:Swine
D000911:Antibodies, Monoclonal; D002966:Clathrin; D010446:Peptide Fragments