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1hx8

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(New page: 200px<br /><applet load="1hx8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hx8, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1hx8.jpg|left|200px]]<br /><applet load="1hx8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hx8.jpg|left|200px]]<br /><applet load="1hx8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hx8, resolution 2.2&Aring;" />
caption="1hx8, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180'''<br />
'''CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HX8 OCA].
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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.]]
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[[Category: Maynard, J.A.]]
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[[Category: Maynard, J A.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
[[Category: Zhang, B.]]
[[Category: Zhang, B.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: coiled-coil]]
[[Category: coiled-coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:52:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:46 2008''

Revision as of 11:05, 21 February 2008


1hx8, resolution 2.2Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180

Overview

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

1HX8 is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.

Reference

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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