1ahq
From Proteopedia
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<StructureSection load='1ahq' size='340' side='right'caption='[[1ahq]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1ahq' size='340' side='right'caption='[[1ahq]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ahq]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ahq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHQ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=1ahq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahq OCA], [https://pdbe.org/1ahq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahq RCSB], [https://www.ebi.ac.uk/pdbsum/1ahq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ACTP_ACACA ACTP_ACACA] Forms a one to one complex with monomeric actin. Can regulate the pool available for polymerization. Severs actin filaments in a dose-dependent manner. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=1ahq ConSurf]. | </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=1ahq ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Actophorin is a member of the actin-depolymerizing factor/cofilin family. It severs actin filaments and sequesters actin monomers. The crystal structure of actophorin will help to elucidate actin-ADF/cofilin interactions. | ||
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| - | Crystal structure of the actin-binding protein actophorin from Acanthamoeba.,Leonard SA, Gittis AG, Petrella EC, Pollard TD, Lattman EE Nat Struct Biol. 1997 May;4(5):369-73. PMID:9145107<ref>PMID:9145107</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ahq" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Acanthamoeba castellanii]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gittis | + | [[Category: Gittis AG]] |
| - | [[Category: Lattman | + | [[Category: Lattman EE]] |
| - | [[Category: Leonard | + | [[Category: Leonard SA]] |
| - | [[Category: Petrella | + | [[Category: Petrella EC]] |
| - | [[Category: Pollard | + | [[Category: Pollard TD]] |
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Current revision
RECOMBINANT ACTOPHORIN
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