Structural domains of clathrin heavy chains.
We used a combination of electron microscopy and proteolytic dissection to study the substructure of the clathrin trimer. The fragments of a heavy chain generated by limited proteolysis of cages were examined by rotary shadowing after disassembly. Correlation of lengths and molecular weights allowed us to map certain cleavage points along an arm and to assign them to positions in a model for a cage. We found that a particularly stable fragment of 52,000-59,000 Mr (depending on the enzyme) corresponded to the knob-like terminal domain at the tip of each arm.
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002966:Clathrin; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D010196:Pancreatic Elastase; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D013381:Subtilisins; D013820:Thermolysin
D002966:Clathrin; D046911:Macromolecular Substances; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D013381:Subtilisins; D010196:Pancreatic Elastase; D013820:Thermolysin