3aco: Difference between revisions
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<StructureSection load='3aco' size='340' side='right'caption='[[3aco]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3aco' size='340' side='right'caption='[[3aco]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3aco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3aco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ACO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ACO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3aco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aco OCA], [https://pdbe.org/3aco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aco RCSB], [https://www.ebi.ac.uk/pdbsum/3aco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aco ProSAT]</span></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=3aco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aco OCA], [https://pdbe.org/3aco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aco RCSB], [https://www.ebi.ac.uk/pdbsum/3aco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aco ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PACN2_HUMAN PACN2_HUMAN] May play a role in endocytosis. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/3aco_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/3aco_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hanawa-Suetsugu | [[Category: Hanawa-Suetsugu K]] | ||
[[Category: Shimada | [[Category: Shimada A]] | ||
[[Category: Shirouzu | [[Category: Shirouzu M]] | ||
[[Category: Suetsugu | [[Category: Suetsugu S]] | ||
[[Category: Terada | [[Category: Terada T]] | ||
[[Category: Umehara | [[Category: Umehara T]] | ||
[[Category: Yamamoto | [[Category: Yamamoto M]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 11:11, 23 October 2024
Crystal structure of the EFC/F-BAR domain of human PACSIN2/Syndapin II (2.7 A)Crystal structure of the EFC/F-BAR domain of human PACSIN2/Syndapin II (2.7 A)
Structural highlights
FunctionPACN2_HUMAN May play a role in endocytosis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation. Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.,Shimada A, Takano K, Shirouzu M, Hanawa-Suetsugu K, Terada T, Toyooka K, Umehara T, Yamamoto M, Yokoyama S, Suetsugu S FEBS Lett. 2010 Mar 19;584(6):1111-8. Epub 2010 Feb 24. PMID:20188097[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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