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1KYU

AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE

Summary for 1KYU
Entry DOI10.2210/pdb1kyu/pdb
Related1KY6 1KY7 1KYD 1KYF 1QTP 1QTS
DescriptorALPHA-ADAPTIN C, EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15 (3 entities in total)
Functional Keywordsprotein-peptide complex, endocytosis, endocytosis-exocytosis complex, endocytosis/exocytosis
Biological sourceMus musculus (house mouse)
More
Cellular locationCell membrane: P17427
Cytoplasm. Isoform 2: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P42567
Total number of polymer chains2
Total formula weight28479.38
Authors
Brett, T.J.,Traub, L.M.,Fremont, D.H. (deposition date: 2002-02-05, release date: 2002-06-12, Last modification date: 2023-08-16)
Primary citationBrett, 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: 12057195
DOI: 10.1016/S0969-2126(02)00784-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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数据于2025-06-11公开中

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