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2v51

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{{Seed}}
 
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[[Image:2v51.jpg|left|200px]]
 
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==Structure of MAL-RPEL1 complexed to actin==
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<StructureSection load='2v51' size='340' side='right'caption='[[2v51]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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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'>[[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>
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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]] 2.35&#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=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>
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{{STRUCTURE_2v51| PDB=2v51 | 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=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>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===STRUCTURE OF MAL-RPEL1 COMPLEXED TO ACTIN===
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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>
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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 2v51" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19008859}}, adds the Publication Abstract to the page
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*[[Actin 3D structures|Actin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19008859 is the PubMed ID number.
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_19008859}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2V51 is a 4 chains structure of sequences from [http://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].
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/19008859 19008859]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Guettler, S.]]
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[[Category: Guettler S]]
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[[Category: Langer, C A.]]
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[[Category: Langer CA]]
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[[Category: Mcdonald, N Q.]]
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[[Category: McDonald NQ]]
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[[Category: Mouilleron, S.]]
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[[Category: Mouilleron S]]
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[[Category: Treisman, R.]]
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[[Category: Treisman R]]
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[[Category: Acetylation]]
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[[Category: Actin]]
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[[Category: Alternative splicing]]
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[[Category: Atp-binding]]
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[[Category: Coiled coil]]
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[[Category: Contractile protein]]
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[[Category: Cytoplasm]]
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[[Category: Cytoskeleton]]
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[[Category: Mal]]
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[[Category: Methylation]]
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[[Category: Muscle protein]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Rpel]]
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[[Category: Structural protein]]
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[[Category: Structural protein/contractile protein]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 27 13:26:19 2008''
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Current revision

Structure of MAL-RPEL1 complexed to actin

PDB ID 2v51

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