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- W1970295512 abstract "The clathrin binding domain of the assembly protein AP-2 has been identified by proteolytically cleaving AP-2 into 2 discrete moieties, termed light and heavy mero-AP (LM-AP and HM-AP), and testing their ability to bind to clathrin assembled into cage structures or to clathrin trimers immobilized on Sepharose. The smaller product (LM-AP), which contains 20–40-kD fragments of the parent 100-kD polypeptides and which comprises two small appendages in the native AP-2 molecule, did not significantly interact with clathrin under either condition. In contrast, the HM-AP complex, which forms the larger central mass of the native AP-2 structure and contains uncleaved 50-kD and 16-kD polypeptides as well as 60–66-kD fragments of the parent 100-kD polypeptides, retained binding activity for both dissociated and assembled clathrin." @default.
- W1970295512 created "2016-06-24" @default.
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- W1970295512 date "1989-01-01" @default.
- W1970295512 modified "2023-10-18" @default.
- W1970295512 title "Identification of the clathrin-binding domain of assembly protein AP-2" @default.
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- W1970295512 doi "https://doi.org/10.1016/s0006-291x(89)80170-6" @default.
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