4b1u
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4b1u is ON HOLD Authors: Mouilleron, S., Wiezlak, M., O'Reilly, N., Treisman, R., McDonald, N.Q. Description: Structure of the Phactr1 RPEL domain ...) |
|||
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Phactr1 RPEL domain and RPEL motif directed assemblies with G-actin reveal the molecular basis for actin binding cooperativity.== | |
| + | <StructureSection load='4b1u' size='340' side='right'caption='[[4b1u]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4b1u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B1U 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]] 2Å</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>, <scene name='pdbligand=LAB:LATRUNCULIN+B'>LAB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1u OCA], [https://pdbe.org/4b1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b1u RCSB], [https://www.ebi.ac.uk/pdbsum/4b1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b1u 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 4b1u" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Actin 3D structures|Actin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: McDonald NQ]] | ||
| + | [[Category: Mouilleron S]] | ||
| + | [[Category: O'Reilly N]] | ||
| + | [[Category: Treisman R]] | ||
| + | [[Category: Wiezlak M]] | ||
Current revision
Structure of the Phactr1 RPEL domain and RPEL motif directed assemblies with G-actin reveal the molecular basis for actin binding cooperativity.
| |||||||||||
