1hx8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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 ...)
Line 1: Line 1:
-
[[Image:1hx8.jpg|left|200px]]<br /><applet load="1hx8" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[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==
-
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.
+
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HX8 OCA].
+
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==
Line 15: Line 15:
[[Category: Chen, J.]]
[[Category: Chen, J.]]
[[Category: Mao, Y.]]
[[Category: Mao, Y.]]
-
[[Category: Maynard, J.A.]]
+
[[Category: Maynard, J A.]]
-
[[Category: Quiocho, F.A.]]
+
[[Category: Quiocho, F A.]]
[[Category: Zhang, B.]]
[[Category: Zhang, B.]]
[[Category: SO4]]
[[Category: SO4]]
Line 23: Line 23:
[[Category: coiled-coil]]
[[Category: coiled-coil]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:52:48 2007''
+
''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

Page seeded by OCA on Thu Feb 21 13:05:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools