1hx8

<table><tr><td colspan='2'>[[1hx8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HX8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1HX8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dvp|1dvp]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1hx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hx8 OCA], [http://pdbe.org/1hx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1hx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hx8 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PICA_DROME PICA_DROME]] Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction.<ref>PMID:9883738</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11239400</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1hx8" style="background-color:#fffaf0;"></div>

[[Category: Drome]]

[[Category: Chen, J]]

[[Category: Mao, Y]]

[[Category: Maynard, J A]]

[[Category: Quiocho, F A]]

[[Category: Zhang, B]]

[[Category: Endocytosis-exocytosis complex]]