1C9I

PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN

Summary for 1C9I

• Entry DOI: 10.2210/pdb1c9i/pdb
• Related: 1C9L
• Descriptor: CLATHRIN, B-ADAPTIN 3 (2 entities in total)
• Functional Keywords: beta-propeller, helical hairpin, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P11442
• Total number of polymer chains: 4
• Total formula weight: 81739.81

Authors

ter Haar, E.,Harrison, S.C.,Kirchhausen, T. (deposition date: 1999-08-02, release date: 2000-02-07, Last modification date: 2024-02-07)

Primary citation

ter Haar, E.,Harrison, S.C.,Kirchhausen, T.
Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin.
Proc.Natl.Acad.Sci.USA, 97:1096-1100, 2000

PubMed 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.

PubMed: 10655490
DOI: 10.1073/pnas.97.3.1096

Experimental method

X-RAY DIFFRACTION (2.9 Å)