1hx8
From Proteopedia
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|PDB= 1hx8 |SIZE=350|CAPTION= <scene name='initialview01'>1hx8</scene>, resolution 2.2Å | |PDB= 1hx8 |SIZE=350|CAPTION= <scene name='initialview01'>1hx8</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= LAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | |GENE= LAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dvp|1dvp]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hx8 OCA], [http://www.ebi.ac.uk/pdbsum/1hx8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hx8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
[[Category: Zhang, B.]] | [[Category: Zhang, B.]] | ||
| - | [[Category: SO4]] | ||
[[Category: all alpha]] | [[Category: all alpha]] | ||
[[Category: alpha helices repeat]] | [[Category: alpha helices repeat]] | ||
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:36 2008'' |
Revision as of 18:11, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | LAP (Drosophila melanogaster) | ||||||
| Related: | 1dvp
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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