1e42: Difference between revisions
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[[Image:1e42.gif|left|200px]] | [[Image:1e42.gif|left|200px]] | ||
'''BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2''' | {{Structure | ||
|PDB= 1e42 |SIZE=350|CAPTION= <scene name='initialview01'>1e42</scene>, resolution 1.70Å | |||
|SITE= <scene name='pdbsite=AC1:Mo5+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC1</scene>, <scene name='pdbsite=AC2:Mo5+Binding+Site+For+Chain+B+Symmetry+Related+Subunits+C+...'>AC2</scene>, <scene name='pdbsite=AC3:Mo5+Binding+Site+For+Chain+B+Symmetry+Related+Subunits+C+...'>AC3</scene>, <scene name='pdbsite=AC4:Mo5+Binding+Site+For+Chain+B+Symmetry+Related+Subunits+C+...'>AC4</scene> and <scene name='pdbsite=AC5:Nik+Binding+Site+For+Chain+B+Symmetry+Related+Subunits+C+...'>AC5</scene> | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E42 is a [ | 1E42 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E42 OCA]. | ||
==Reference== | ==Reference== | ||
The structure and function of the beta 2-adaptin appendage domain., Owen DJ, Vallis Y, Pearse BM, McMahon HT, Evans PR, EMBO J. 2000 Aug 15;19(16):4216-27. PMID:[http:// | The structure and function of the beta 2-adaptin appendage domain., Owen DJ, Vallis Y, Pearse BM, McMahon HT, Evans PR, EMBO J. 2000 Aug 15;19(16):4216-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10944104 10944104] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: endocytosis]] | [[Category: endocytosis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:49:19 2008'' | ||
Revision as of 11:49, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Sites: | , , , and | ||||||
| Ligands: | , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2
OverviewOverview
The heterotetrameric AP2 adaptor (alpha, beta 2, mu 2 and sigma 2 subunits) plays a central role in clathrin-mediated endocytosis. We present the protein recruitment function and 1.7 A resolution structure of its beta 2-appendage domain to complement those previously determined for the mu 2 subunit and alpha appendage. Using structure-directed mutagenesis, we demonstrate the ability of the beta 2 appendage alone to bind directly to clathrin and the accessory proteins AP180, epsin and eps15 at the same site. Clathrin polymerization is promoted by binding of clathrin simultaneously to the beta 2-appendage site and to a second site on the adjacent beta 2 hinge. This results in the displacement of the other ligands from the beta 2 appendage. Thus clathrin binding to an AP2-accessory protein complex would cause the controlled release of accessory proteins at sites of vesicle formation.
About this StructureAbout this Structure
1E42 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The structure and function of the beta 2-adaptin appendage domain., Owen DJ, Vallis Y, Pearse BM, McMahon HT, Evans PR, EMBO J. 2000 Aug 15;19(16):4216-27. PMID:10944104
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