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

authors

ter Haar E,Harrison SC,Kirchhausen T

keywords:

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

1096-100

issue

3

eissn

0027-8424

issn

1091-6490

journal_volume

97

pub_type

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