1kyu
From Proteopedia
(New page: 200px<br /><applet load="1kyu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kyu, resolution 1.80Å" /> '''AP-2 CLATHRIN ADAPTO...) |
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- | [[Image:1kyu.jpg|left|200px]]<br /><applet load="1kyu" size=" | + | [[Image:1kyu.jpg|left|200px]]<br /><applet load="1kyu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kyu, resolution 1.80Å" /> | caption="1kyu, resolution 1.80Å" /> | ||
'''AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE'''<br /> | '''AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
- | Clathrin-mediated endocytosis depends upon the interaction of accessory | + | 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== | ==About this Structure== | ||
- | 1KYU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1KYU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
- | [[Category: Brett, T | + | [[Category: Brett, T J.]] |
- | [[Category: Fremont, D | + | [[Category: Fremont, D H.]] |
- | [[Category: Traub, L | + | [[Category: Traub, L M.]] |
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:22 2008'' |
Revision as of 11:39, 21 February 2008
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AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE
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
1KYU is a Protein complex structure of sequences from Mus musculus. 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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