4b1v: Difference between revisions
New page: '''Unreleased structure''' The entry 4b1v is ON HOLD Authors: Mouilleron, S., Wiezlak, M., O'Reilly, N., Treisman, R., McDonald, N.Q. Description: Structure of the Phactr1 RPEL-N domai... |
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The | ==Structure of the Phactr1 RPEL-N domain bound to G-actin== | ||
<StructureSection load='4b1v' size='340' side='right'caption='[[4b1v]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b1v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B1V FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LAB:LATRUNCULIN+B'>LAB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4b1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1v OCA], [https://pdbe.org/4b1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b1v RCSB], [https://www.ebi.ac.uk/pdbsum/4b1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b1v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PHAR1_MOUSE PHAR1_MOUSE] Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival (By similarity). Plays a role in cell motility.<ref>PMID:22976292</ref> <ref>PMID:23041370</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Phactr family of PP1-binding proteins and the myocardin-related transcription factor family of transcriptional coactivators contain regulatory domains comprising three copies of the RPEL motif, a G-actin binding element. We report the structure of a Phactr1 G-actinRPEL domain complex. Three G-actins surround the crank-shaped RPEL domain forming a closed helical assembly. Their spatial relationship is identical to the RPEL-actins within the pentavalent MRTF G-actinRPEL domain complex, suggesting that conserved cooperative interactions between actinRPEL units organize the assembly. In the trivalent Phactr1 complex, each G-actinRPEL unit makes secondary contacts with its downstream actin involving distinct RPEL residues. Similar secondary contacts are seen in G-actinRPEL peptide crystals. Loss-of-secondary-contact mutations destabilize the Phactr1 G-actinRPEL assembly. Furthermore, actin-mediated inhibition of Phactr1 nuclear import requires secondary contact residues in the Phactr1 N-terminal RPEL-N motif, suggesting that it involves interaction of RPEL-N with the C-terminal assembly. Secondary actin contacts by actin-bound RPEL motifs thus govern formation of multivalent actinRPEL assemblies. | |||
Structures of the Phactr1 RPEL Domain and RPEL Motif Complexes with G-Actin Reveal the Molecular Basis for Actin Binding Cooperativity.,Mouilleron S, Wiezlak M, O'Reilly N, Treisman R, McDonald NQ Structure. 2012 Oct 2. pii: S0969-2126(12)00335-8. doi:, 10.1016/j.str.2012.08.031. PMID:23041370<ref>PMID:23041370</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4b1v" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Actin 3D structures|Actin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: McDonald NQ]] | |||
[[Category: Mouilleron S]] | |||
[[Category: O'Reilly N]] | |||
[[Category: Treisman R]] | |||
[[Category: Wiezlak M]] | |||
Latest revision as of 14:41, 20 December 2023
Structure of the Phactr1 RPEL-N domain bound to G-actinStructure of the Phactr1 RPEL-N domain bound to G-actin
Structural highlights
FunctionPHAR1_MOUSE Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival (By similarity). Plays a role in cell motility.[1] [2] Publication Abstract from PubMedThe Phactr family of PP1-binding proteins and the myocardin-related transcription factor family of transcriptional coactivators contain regulatory domains comprising three copies of the RPEL motif, a G-actin binding element. We report the structure of a Phactr1 G-actinRPEL domain complex. Three G-actins surround the crank-shaped RPEL domain forming a closed helical assembly. Their spatial relationship is identical to the RPEL-actins within the pentavalent MRTF G-actinRPEL domain complex, suggesting that conserved cooperative interactions between actinRPEL units organize the assembly. In the trivalent Phactr1 complex, each G-actinRPEL unit makes secondary contacts with its downstream actin involving distinct RPEL residues. Similar secondary contacts are seen in G-actinRPEL peptide crystals. Loss-of-secondary-contact mutations destabilize the Phactr1 G-actinRPEL assembly. Furthermore, actin-mediated inhibition of Phactr1 nuclear import requires secondary contact residues in the Phactr1 N-terminal RPEL-N motif, suggesting that it involves interaction of RPEL-N with the C-terminal assembly. Secondary actin contacts by actin-bound RPEL motifs thus govern formation of multivalent actinRPEL assemblies. Structures of the Phactr1 RPEL Domain and RPEL Motif Complexes with G-Actin Reveal the Molecular Basis for Actin Binding Cooperativity.,Mouilleron S, Wiezlak M, O'Reilly N, Treisman R, McDonald NQ Structure. 2012 Oct 2. pii: S0969-2126(12)00335-8. doi:, 10.1016/j.str.2012.08.031. PMID:23041370[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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