1ky6
AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE
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OverviewOverview
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.
About this StructureAbout this Structure
1KY6 is a Protein complex structure of sequences from Mus musculus with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Accessory protein recruitment motifs in clathrin-mediated endocytosis., Brett TJ, Traub LM, Fremont DH, Structure. 2002 Jun;10(6):797-809. PMID:12057195
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