3tpq: Difference between revisions

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-{{STRUCTURE_3tpq|  PDB=3tpq  |  SCENE=  }}
-===Crystal structure of wild-type MAL RPEL domain in complex with five G-actins===
-{{ABSTRACT_PUBMED_21964294}}
-==Function==
+==Crystal structure of wild-type MAL RPEL domain in complex with five G-actins==
-[[http://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.
+<StructureSection load='3tpq' size='340' side='right'caption='[[3tpq]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3tpq]] is a 6 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=3TPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TPQ 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]] 3.45&#8491;</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></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=3tpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tpq OCA], [https://pdbe.org/3tpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tpq RCSB], [https://www.ebi.ac.uk/pdbsum/3tpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tpq 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 ==
+The coordination of cytoskeletal actin dynamics with gene expression reprogramming is emerging as a crucial mechanism to control diverse cellular processes, including cell migration, differentiation and neuronal circuit assembly. The actin-binding transcriptional coactivator MAL (also known as MRTF-A/MKL1/BSAC) senses G-actin concentration and transduces Rho GTPase signals to serum response factor (SRF). MAL rapidly shuttles between the cytoplasm and the nucleus in unstimulated cells but Rho-induced depletion of G-actin leads to MAL nuclear accumulation and activation of transcription of SRF:MAL-target genes. Although the molecular and structural basis of actin-regulated nucleocytoplasmic shuttling of MAL is not understood fully, it is proposed that nuclear import of MAL is mediated by importin alpha/beta heterodimer, and that G-actin competes with importin alpha/beta for the binding to MAL. Here we present structural, biochemical and cell biological evidence that MAL has a classical bipartite nuclear localization signal (NLS) in the N-terminal 'RPEL' domain containing Arg-Pro-X-X-X-Glu-Leu (RPEL) motifs. The NLS residues of MAL adopt an extended conformation and bind along the surface groove of importin-alpha, interacting with the major- and minor-NLS binding sites. We also present a crystal structure of wild-type MAL RPEL domain in complex with five G-actins. Comparison of the importin-alpha- and actin-complexes revealed that the binding of G-actins to MAL is associated with folding of NLS residues into a helical conformation that is inappropriate for importin-alpha recognition.
-==About this Structure==
+Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL.,Hirano H, Matsuura Y Biochem Biophys Res Commun. 2011 Oct 22;414(2):373-8. doi:, 10.1016/j.bbrc.2011.09.079. Epub 2011 Sep 21. PMID:21964294<ref>PMID:21964294</ref>
-[[3tpq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TPQ OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:021964294</ref><references group="xtra"/><references/>
+</div>
+<div class="pdbe-citations 3tpq" 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: Hirano, H.]]
+[[Category: Hirano H]]
-[[Category: Matsuura, Y.]]
+[[Category: Matsuura Y]]
-[[Category: Contractile protein-transcription complex]]
-[[Category: Regulation of nuclear import]]