From the Cover: Peptide-in-groove interactions link target proteins to the -propeller of clathrin
Abstract
The "WD40" domain is a widespread recognition module for linking partner proteins in intracellular networks of signaling and sorting. The clathrin amino-terminal domain, which directs incorporation of cargo into coated pits, is a β-propeller closely related in structure to WD40 modules. The crystallographically determined structures of complexes of the clathrin-terminal domain with peptides derived from two different cargo adaptors, β-arrestin 2 and the β-subunit of the AP-3 complex, reveal strikingly similar peptide-in-groove interactions. The two peptides in our structures contain related, five-residue motifs, which form the core of their contact with clathrin. A number of other proteins involved in endocytosis have similar "clathrin-box" motifs, and it therefore is likely that they all bind the terminal domain in the same way. We propose that a peptide-in-groove interaction is an important general mode by which β-propellers recognize specific target proteins.
- Publication:
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Proceedings of the National Academy of Science
- Pub Date:
- February 2000
- DOI:
- 10.1073/pnas.97.3.1096
- Bibcode:
- 2000PNAS...97.1096T
- Keywords:
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- Cell Biology