2vk3

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{{Seed}}
 
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[[Image:2vk3.png|left|200px]]
 
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==Crystal structure of rat profilin 2a==
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The line below this paragraph, containing "STRUCTURE_2vk3", creates the "Structure Box" on the page.
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<StructureSection load='2vk3' size='340' side='right'caption='[[2vk3]], [[Resolution|resolution]] 1.70&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'>[[2vk3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VK3 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]] 1.7&#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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2vk3| PDB=2vk3 | 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=2vk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk3 OCA], [https://pdbe.org/2vk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vk3 RCSB], [https://www.ebi.ac.uk/pdbsum/2vk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vk3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PROF2_RAT PROF2_RAT] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
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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/vk/2vk3_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=2vk3 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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Profilins are key regulators of the actin microfilament system and in neuronal tissues the profilin 2a isoform is the most abundant and important profilin. The high-resolution crystal structure of rat profilin 2a has been determined in the absence of ligands. By comparing the structure with those of peptide-liganded profilin 2a and unliganded profilin 2b, it can be concluded that the binding site for proline-rich peptides is pre-organized. The C-terminus of profilin 2a is also well ordered in the absence of ligand peptide, in contrast to the 2b isoform which is generated by alternative splicing. Covalent modifications of four cysteine residues were also detected in profilin 2a, as well as a number of other modifications in profilin 2 from rat brain; such modifications could significantly affect the function of profilin. It was also shown that profilin 2a binds to the neuronal protein palladin, including a synthetic palladin peptide; peptides from another profilin ligand, dynamin 1, failed to interact with both profilin 1 and profilin 2a. These results allow a better understanding of the structure-function relationships and ligand binding of mammalian profilin 2a.
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===CRYSTAL STRUCTURE OF RAT PROFILIN 2A===
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Structure, modifications and ligand-binding properties of rat profilin 2a.,Haikarainen T, Chen WQ, Lubec G, Kursula P Acta Crystallogr D Biol Crystallogr. 2009 Apr;65(Pt 4):303-11. Epub 2009, Mar 19. PMID:19307711<ref>PMID:19307711</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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<div class="pdbe-citations 2vk3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19307711}}, adds the Publication Abstract to the page
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*[[Profilin 3D Structures|Profilin 3D Structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19307711 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19307711}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2VK3 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK3 OCA].
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==Reference==
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<ref group="xtra">PMID:19307711</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Haikarainen, T.]]
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[[Category: Haikarainen T]]
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[[Category: Kursula, P.]]
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[[Category: Kursula P]]
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[[Category: Acetylation]]
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[[Category: Actin-binding]]
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[[Category: Alternative splicing]]
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[[Category: Cytoplasm]]
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[[Category: Cytoskeleton]]
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[[Category: Disulfide bridge]]
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[[Category: Profilin]]
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[[Category: Protein-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 8 20:07:39 2009''
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Current revision

Crystal structure of rat profilin 2a

PDB ID 2vk3

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