1cnu

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{{Seed}}
 
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[[Image:1cnu.png|left|200px]]
 
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==PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA==
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The line below this paragraph, containing "STRUCTURE_1cnu", creates the "Structure Box" on the page.
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<StructureSection load='1cnu' size='340' side='right'caption='[[1cnu]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1cnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_polyphaga Acanthamoeba polyphaga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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{{STRUCTURE_1cnu| PDB=1cnu | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnu OCA], [https://pdbe.org/1cnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cnu RCSB], [https://www.ebi.ac.uk/pdbsum/1cnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/1cnu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1cnu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acanthamoeba actophorin is a member of ADF/cofilin family that binds both actin monomers and filaments. We used fluorescence anisotropy to study the interaction of actin monomers with recombinant actophorin labeled with rhodamine on a cysteine substituted for Serine-88. Labeled actophorin retains its affinity for actin and ability to reduce the low shear viscosity of actin filaments. At physiological ionic strength, actophorin binds Mg-ADP-actin monomers (Kd = 0.1 microM) 40 times stronger than Mg-ATP-actin monomers. When bound to actin monomers, actophorin has no effect on elongation at either end of actin filaments by Mg-ATP-actin and slightly increases the rate of elongation at both ends by Mg-ADP-actin. Thus actophorin does not sequester actin monomers. Sedimentation equilibrium ultracentrifugation shows that actophorin and profilin compete for binding actin monomers. Actophorin and profilin have opposite effects on the rate of exchange of nucleotide bound to actin monomers. Despite the high affinity of actophorin for ADP-actin, physiological concentrations of profilin overcome the inhibition of ADP exchange by actophorin. Profilin rapidly recycles ADP-actin back to the profilin-ATP-actin pool ready for elongation of actin filaments.
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===PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA===
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Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin.,Blanchoin L, Pollard TD J Biol Chem. 1998 Sep 25;273(39):25106-11. PMID:9737968<ref>PMID:9737968</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_9737968}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1cnu" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9737968 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9737968}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1CNU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_polyphaga Acanthamoeba polyphaga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNU OCA].
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==Reference==
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Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin., Blanchoin L, Pollard TD, J Biol Chem. 1998 Sep 25;273(39):25106-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9737968 9737968]
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[[Category: Acanthamoeba polyphaga]]
[[Category: Acanthamoeba polyphaga]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blanchoin, L.]]
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[[Category: Blanchoin L]]
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[[Category: Choe, S.]]
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[[Category: Choe S]]
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[[Category: Pollard, T D.]]
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[[Category: Pollard TD]]
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[[Category: Robinson, R C.]]
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[[Category: Robinson RC]]
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[[Category: Actin-binding protein]]
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[[Category: Adf]]
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[[Category: Cofilin]]
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[[Category: Contractile]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:59:58 2008''
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Current revision

PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA

PDB ID 1cnu

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