Work

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

Year: 2000

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.97.3.1096

Authors: Ernst ter Haar, Stephen C. Harrison, Tomas Kirchhausen

Institutions: Howard Hughes Medical Institute, Harvard University

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: Molecular Interactions in Clathrin Coated Vesicles, G7314885031