1KY6

AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE

Summary for 1KY6

• Entry DOI: 10.2210/pdb1ky6/pdb
• Related: 1KY7 1KYD 1KYF 1KYU 1QTP 1QTS
• Descriptor: ALPHA-ADAPTIN C, EH DOMAIN BINDING PROTEIN EPSIN, SULFATE ION, ... (4 entities in total)
• Functional Keywords: protein-peptide complex, endocytosis, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane: P17427; Cytoplasm: O88339
• Total number of polymer chains: 2
• Total formula weight: 28689.52

Authors

Brett, T.J.,Traub, L.M.,Fremont, D.H. (deposition date: 2002-02-03, release date: 2002-06-12, Last modification date: 2023-08-16)

Primary citation

Brett, T.J.,Traub, L.M.,Fremont, D.H.
Accessory protein recruitment motifs in clathrin-mediated endocytosis.
Structure, 10:797-809, 2002

PubMed Abstract: Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the alpha-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I beta turn conformations to a conserved pocket on the alpha-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.

PubMed: 12057195
DOI: 10.1016/S0969-2126(02)00784-0

Experimental method

X-RAY DIFFRACTION (2 Å)