1hx8: Difference between revisions

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 ==CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF DROSOPHILA AP180==
-<StructureSection load='1hx8' size='340' side='right' caption='[[1hx8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='1hx8' size='340' side='right'caption='[[1hx8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HX8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hx8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. 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 [https://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"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dvp|1dvp]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=1hx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hx8 OCA], [https://pdbe.org/1hx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hx8 RCSB], [https://www.ebi.ac.uk/pdbsum/1hx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hx8 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://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>
 </table>
 == Function ==
-[[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>
+[https://www.uniprot.org/uniprot/PICAL_DROME PICAL_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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hx8 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== 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>
-</div>
-<div class="pdbe-citations 1hx8" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
-[[Category: Chen, J]]
+[[Category: Large Structures]]
-[[Category: Mao, Y]]
+[[Category: Chen J]]
-[[Category: Maynard, J A]]
+[[Category: Mao Y]]
-[[Category: Quiocho, F A]]
+[[Category: Maynard JA]]
-[[Category: Zhang, B]]
+[[Category: Quiocho FA]]
-[[Category: All alpha]]
+[[Category: Zhang B]]
-[[Category: Alpha helices repeat]]
-[[Category: Coiled-coil]]
-[[Category: Endocytosis-exocytosis complex]]