1ky7
From Proteopedia
(New page: 200px<br /> <applet load="1ky7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ky7, resolution 2.15Å" /> '''THE AP-2 CLATHRIN A...) |
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| - | [[Image:1ky7.gif|left|200px]]<br /> | + | [[Image:1ky7.gif|left|200px]]<br /><applet load="1ky7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ky7" size=" | + | |
caption="1ky7, resolution 2.15Å" /> | caption="1ky7, resolution 2.15Å" /> | ||
'''THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF'''<br /> | '''THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF'''<br /> | ||
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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== | ||
| + | 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== | ||
| - | 1KY7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 1KY7 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb88_1.html Clathrin]]. Full crystallographic information is available from [http:// | + | 1KY7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 1KY7 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb88_1.html Clathrin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:15:37 2008'' |
Revision as of 14:15, 15 February 2008
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THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF
Contents |
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.
Disease
Known disease associated with this structure: Myopathy, centronuclear, autosomal recessive OMIM:[601248]
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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