3u9d

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==Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP==
==Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP==
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<StructureSection load='3u9d' size='340' side='right' caption='[[3u9d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3u9d' size='340' side='right'caption='[[3u9d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u9d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u9d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9D FirstGlance]. <br>
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</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sjh|3sjh]], [[3u8x|3u8x]], [[1sqk|1sqk]], [[3u9z|3u9z]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sjh|3sjh]], [[3u8x|3u8x]], [[1sqk|1sqk]], [[3u9z|3u9z]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TMSB4, THYB4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TMSB4, THYB4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
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<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=3u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9d OCA], [http://pdbe.org/3u9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u9d RCSB], [http://www.ebi.ac.uk/pdbsum/3u9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9d ProSAT]</span></td></tr>
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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=3u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9d OCA], [https://pdbe.org/3u9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9d RCSB], [https://www.ebi.ac.uk/pdbsum/3u9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACTS_RAT ACTS_RAT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/TYB4_BOVIN TYB4_BOVIN]] Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase.
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[[https://www.uniprot.org/uniprot/ACTS_RAT ACTS_RAT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[https://www.uniprot.org/uniprot/TYB4_BOVIN TYB4_BOVIN]] Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 3u9d" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3u9d" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Actin 3D structures|Actin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Drome]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Carlier, M F]]
[[Category: Carlier, M F]]

Revision as of 06:03, 13 July 2022

Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP

PDB ID 3u9d

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