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Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1096-100.

Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin.

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  • 1Howard Hughes Medical Institute and Children's Hospital, Laboratory of Molecular Medicine, Harvard Medical School, Boston, MA 02115, USA.

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 beta-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, beta-arrestin 2 and the beta-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 beta-propellers recognize specific target proteins.

Comment in

  • A groovy new structure. [Proc Natl Acad Sci U S A. 2000]
PMID:
10655490
[PubMed - indexed for MEDLINE]
PMCID:
PMC15533
Free PMC Article

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