The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
Open accessAbstract
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.
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Self-citationTHE ESCRT COMPLEXES: Structure and Mechanism of a Membrane-Trafficking Network
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Metadata
- Authors
- ter Haar, E., Harrison, S. C., & Kirchhausen, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-02
- Volume
- 97
- Issue
- 3
- Pages
- 1096-1100
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1972087498
- Cited by
- 290
- References
- 52
- FWCI
- 9.23
- Type
- journal article
- Language
- en
- Open access
- green
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- ter Haar, E., Harrison, S. C., & Kirchhausen, T. (2000). Peptide-in-groove interactions link target proteins to the β-propeller of clathrin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.3.1096
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