2v51

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(Difference between revisions)

Revision as of 15:27, 5 August 2016

STRUCTURE OF MAL-RPEL1 COMPLEXED TO ACTIN

Structural highlights

2v51 is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1lcu, 2a42, 2aso, 1ijj, 1wua, 1o1a, 1o18, 1m8q, 1rfq, 1uy5, 1ma9, 2d1k, 1rdw, 1o1b, 1o1d, 2a40, 2a5x, 1qz5, 1nwk, 1j6z, 1sqk, 1atn, 1s22, 1t44, 2ff3, 1eqy, 1mvw, 2ff6, 2fxu, 1o1f, 1kxp, 2asp, 1rgi, 1o19, 1y64, 1alm, 1o1e, 1esv, 1p8z, 1h1v, 1o1c, 2vcp, 1o1g, 2a3z, 1lot, 2asm, 2a41, 1qz6, 2vyp, 2v52
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. EMBO J. 2008 Nov 13. PMID:19008859 doi:emboj2008235

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v51"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF MAL-RPEL1 COMPLEXED TO ACTIN==
 <StructureSection load='2v51' size='340' side='right' caption='[[2v51]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lcu|1lcu]], [[2a42|2a42]], [[2aso|2aso]], [[1ijj|1ijj]], [[1wua|1wua]], [[1o1a|1o1a]], [[1o18|1o18]], [[1m8q|1m8q]], [[1rfq|1rfq]], [[1uy5|1uy5]], [[1ma9|1ma9]], [[2d1k|2d1k]], [[1rdw|1rdw]], [[1o1b|1o1b]], [[1o1d|1o1d]], [[2a40|2a40]], [[2a5x|2a5x]], [[1qz5|1qz5]], [[1nwk|1nwk]], [[1j6z|1j6z]], [[1sqk|1sqk]], [[1atn|1atn]], [[1s22|1s22]], [[1t44|1t44]], [[2ff3|2ff3]], [[1eqy|1eqy]], [[1mvw|1mvw]], [[2ff6|2ff6]], [[2fxu|2fxu]], [[1o1f|1o1f]], [[1kxp|1kxp]], [[2asp|2asp]], [[1rgi|1rgi]], [[1o19|1o19]], [[1y64|1y64]], [[1alm|1alm]], [[1o1e|1o1e]], [[1esv|1esv]], [[1p8z|1p8z]], [[1h1v|1h1v]], [[1o1c|1o1c]], [[2vcp|2vcp]], [[1o1g|1o1g]], [[2a3z|2a3z]], [[1lot|1lot]], [[2asm|2asm]], [[2a41|2a41]], [[1qz6|1qz6]], [[2vyp|2vyp]], [[2v52|2v52]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v51 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v51 RCSB], [http://www.ebi.ac.uk/pdbsum/2v51 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v51 OCA], [http://pdbe.org/2v51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v51 RCSB], [http://www.ebi.ac.uk/pdbsum/2v51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v51 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2v51" style="background-color:#fffaf0;"></div>
 ==See Also==

2v51

From Proteopedia

Revision as of 15:27, 5 August 2016

STRUCTURE OF MAL-RPEL1 COMPLEXED TO ACTIN

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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