1ky7

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|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1qtp|1QTP]], [[1qts|1QTS]], [[1ky6|1KY6]], [[1ky7|1KY7]], [[1kyd|1KYD]], [[1kyf|1KYF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ky7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky7 OCA], [http://www.ebi.ac.uk/pdbsum/1ky7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ky7 RCSB]</span>
}}
}}
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==Overview==
==Overview==
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.
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.
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==Disease==
 
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Known disease associated with this structure: Myopathy, centronuclear, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601248 601248]]
 
==About this Structure==
==About this Structure==
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[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:23:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:55:19 2008''

Revision as of 18:55, 30 March 2008


PDB ID 1ky7

Drag the structure with the mouse to rotate
, resolution 2.15Å
Related: 1QTP, 1QTS, 1KY6, 1KY7, 1KYD, 1KYF


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF


Overview

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 Structure

1KY7 is a Protein complex structure of sequences from Mus musculus. The following page contains interesting information on the relation of 1KY7 with [Clathrin]. Full crystallographic information is available from OCA.

Reference

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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