1hx8: Difference between revisions
New page: left|200px<br /><applet load="1hx8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hx8, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1hx8.jpg|left|200px]]<br /><applet load="1hx8" size=" | [[Image:1hx8.jpg|left|200px]]<br /><applet load="1hx8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hx8, resolution 2.2Å" /> | caption="1hx8, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180'''<br /> | '''CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180'''<br /> | ||
==Overview== | ==Overview== | ||
Clathrin-mediated endocytosis plays a major role in retrieving synaptic | Clathrin-mediated endocytosis plays a major role in retrieving synaptic vesicles from the plasma membrane following exocytosis. This endocytic process requires AP180 (or a homolog), which promotes the assembly and restricts the size of clathrin-coated vesicles. The highly conserved 33 kDa amino-terminal domain of AP180 plays a critical role in binding to phosphoinositides and in regulating the clathrin assembly activity of AP180. The crystal structure of the amino-terminal domain reported herein reveals a novel fold consisting of a large double layer of sheets of ten alpha helices and a unique site for binding phosphoinositides. The finding that the clathrin-box motif is mostly buried and lies in a helix indicates a different site and mechanism for binding of the domain to clathrins than previously assumed. | ||
==About this Structure== | ==About this Structure== | ||
1HX8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1HX8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HX8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Chen, J.]] | [[Category: Chen, J.]] | ||
[[Category: Mao, Y.]] | [[Category: Mao, Y.]] | ||
[[Category: Maynard, J | [[Category: Maynard, J A.]] | ||
[[Category: Quiocho, F | [[Category: Quiocho, F A.]] | ||
[[Category: Zhang, B.]] | [[Category: Zhang, B.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:46 2008'' | ||
Revision as of 14:05, 21 February 2008
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CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180
OverviewOverview
Clathrin-mediated endocytosis plays a major role in retrieving synaptic vesicles from the plasma membrane following exocytosis. This endocytic process requires AP180 (or a homolog), which promotes the assembly and restricts the size of clathrin-coated vesicles. The highly conserved 33 kDa amino-terminal domain of AP180 plays a critical role in binding to phosphoinositides and in regulating the clathrin assembly activity of AP180. The crystal structure of the amino-terminal domain reported herein reveals a novel fold consisting of a large double layer of sheets of ten alpha helices and a unique site for binding phosphoinositides. The finding that the clathrin-box motif is mostly buried and lies in a helix indicates a different site and mechanism for binding of the domain to clathrins than previously assumed.
About this StructureAbout this Structure
1HX8 is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis., Mao Y, Chen J, Maynard JA, Zhang B, Quiocho FA, Cell. 2001 Feb 9;104(3):433-40. PMID:11239400
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