3u4l

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u4l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U4L FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u4l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U4L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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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]] 2.4&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3u4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u4l OCA], [https://pdbe.org/3u4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u4l RCSB], [https://www.ebi.ac.uk/pdbsum/3u4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u4l 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=3u4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u4l OCA], [https://pdbe.org/3u4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u4l RCSB], [https://www.ebi.ac.uk/pdbsum/3u4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u4l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ACTB_BOVIN ACTB_BOVIN]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[https://www.uniprot.org/uniprot/PROF1_BOVIN PROF1_BOVIN]] 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. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR (By similarity).
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[https://www.uniprot.org/uniprot/ACTB_BOVIN ACTB_BOVIN] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Actin is a ubiquitous eukaryotic protein that is responsible for cellular scaffolding, motility, and division. The ability of actin to form a helical filament is the driving force behind these cellular activities. Formation of a filament depends on the successful exchange of actin's ADP for ATP. Mammalian profilin is a small actin binding protein that catalyzes the exchange of nucleotide and facilitates the addition of an actin monomer to a growing filament. Here, crystal structures of profilin-actin have been determined to show an actively exchanging ATP. Structural analysis shows how the binding of profilin to the barbed end of actin causes a rotation of the small domain relative to the large domain. This conformational change is propagated to the ATP site and causes a shift in nucleotide loops, which in turn causes a repositioning of Ca(2+) to its canonical position as the cleft closes around ATP. Reversal of the solvent exposure of Trp356 is also involved in cleft closure. In addition, secondary calcium binding sites were identified.
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Structural basis for profilin-mediated actin nucleotide exchange.,Porta JC, Borgstahl GE J Mol Biol. 2012 Apr 20;418(1-2):103-16. Epub 2012 Feb 22. PMID:22366544<ref>PMID:22366544</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 3u4l" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Actin 3D structures|Actin 3D structures]]
*[[Profilin 3D Structures|Profilin 3D Structures]]
*[[Profilin 3D Structures|Profilin 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Borgstahl, G E]]
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[[Category: Borgstahl GE]]
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[[Category: Porta, J C]]
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[[Category: Porta JC]]
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[[Category: Atpase]]
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[[Category: Structural protein]]
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Revision as of 13:48, 14 March 2024

Cryocooled bovine profilin:actin crystal structure to 2.4 A

PDB ID 3u4l

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