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THE CONFORMATION OF CLATHRIN LIGHT‐CHAINS ON TRISKELIONS PROBED BY ANTIBODY INHIBITION
Author(s) -
JACKSON A. P.
Publication year - 1996
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1996.0046
Subject(s) - immunoglobulin light chain , clathrin , epitope , amino terminal , chemistry , biophysics , monoclonal antibody , antibody , stereochemistry , side chain , peptide , biochemistry , peptide sequence , microbiology and biotechnology , biology , endocytosis , receptor , genetics , gene , organic chemistry , polymer
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.