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2v51
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2v51 is ON HOLD Authors: Mouilleron, S., Guettler, S., Langer, C.A., Treisman, R., Mcdonald, N.Q. Description: Structure of MAL-RPEL1 complexed to ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of MAL-RPEL1 complexed to actin== | |
| + | <StructureSection load='2v51' size='340' side='right'caption='[[2v51]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2v51]] 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=2V51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V51 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]] 2.35Å</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=2v51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v51 OCA], [https://pdbe.org/2v51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v51 RCSB], [https://www.ebi.ac.uk/pdbsum/2v51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v51 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Serum response factor transcriptional activity is controlled through interactions with regulatory cofactors such as the coactivator MAL/MRTF-A (myocardin-related transcription factor A). MAL is itself regulated in vivo by changes in cellular actin dynamics, which alter its interaction with G-actin. The G-actin-sensing mechanism of MAL/MRTF-A resides in its N-terminal domain, which consists of three tandem RPEL repeats. We describe the first molecular insights into RPEL function obtained from structures of two independent RPEL(MAL) peptide:G-actin complexes. Both RPEL peptides bind to the G-actin hydrophobic cleft and to subdomain 3. These RPEL(MAL):G-actin structures explain the sequence conservation defining the RPEL motif, including the invariant arginine. Characterisation of the RPEL(MAL):G-actin interaction by fluorescence anisotropy and cell reporter-based assays validates the significance of actin-binding residues for proper MAL localisation and regulation in vivo. We identify important differences in G-actin engagement between the two RPEL(MAL) structures. Comparison with other actin-binding proteins reveals an unexpected similarity to the vitamin-D-binding protein, extending the G-actin-binding protein repertoire. | ||
| - | + | Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.,Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ EMBO J. 2008 Nov 13. PMID:19008859<ref>PMID:19008859</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2v51" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Actin 3D structures|Actin 3D structures]] | ||
| + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Guettler S]] | ||
| + | [[Category: Langer CA]] | ||
| + | [[Category: McDonald NQ]] | ||
| + | [[Category: Mouilleron S]] | ||
| + | [[Category: Treisman R]] | ||
Current revision
Structure of MAL-RPEL1 complexed to actin
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