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 Cited by 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: 12057195DOI: 10.1016/S0969-2126(02)00784-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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