Crystallographic study of cytochrome b 562 from Escherichia coli.
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Ammonium Sulfate↗
Biomedical subjects
K Drickamer
Publications and source records attributed to K Drickamer.
Clathrin light chains contain brain-specific insertion sequences and a region of homology with intermediate filaments.
The primary structures of four bovine clathrin light chains have been determined. Light chains LCa and LCb are homologous proteins encoded by different genes. In the brain the messenger RNA from these genes undergoes differential splicing to yield proteins having centrally inserted brain-specific sequences. A potentially alpha-helical region of the clathrin light chains shows homology with intermediate filament proteins.
Amino Acid Sequence↗
Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity.
At least four distinct forms of clathrin light chains are found in mammalian cells. This molecular variability derives from tissue-specific patterns of expression of LCa and LCb genes. Sequence analysis shows an overall homology of 60% between LCa and LCb and the presence of brain-specific insertion sequences. These findings suggest that the different light chains have both shared and specialized functions. To address this question we have used a panel of monoclonal antibodies to identify two structurally and functionally distinct regions in the clathrin light-chain sequences. One region (residues 158-208) is exposed in native clathrin structures (triskelions and coated vesicles) and includes the brain-specific insertion sequences. The second region (residues 93-157), which is cryptic in native clathrin structures, is involved in binding the clathrin heavy chain and contains the region of strongest homology with intermediate filament proteins.
Adrenal Glands↗