1hx8
From Proteopedia
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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 SO4 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 Tue Nov 20 16:52:48 2007
