View source for 9tga


==Drebrin actin binding domain 2 bound to F-actin==
<StructureSection load='9tga' size='340' side='right'caption='[[9tga]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9tga]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=9TGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9TGA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.29&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9tga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9tga OCA], [https://pdbe.org/9tga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9tga RCSB], [https://www.ebi.ac.uk/pdbsum/9tga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9tga ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DREB_HUMAN DREB_HUMAN] Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.<ref>PMID:20215400</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Drebrin modulates F-actin networks and links them to other intracellular components, regulating crucial processes including neuritogenesis, synaptic plasticity, virus internalisation and cancer invasion. Using single-particle cryo-EM we characterise drebrin's interaction with F-actin through two separate conserved actin binding domains (ABD1 and ABD2), revealing structural bases for its F-actin-modulating properties. We describe a multimodal interaction where drebrin's ABD1 can adopt two conformations and a long flexible loop connecting to ABD2 allows the two ABDs to occupy multiple relative positions along F-actin. The flexible loop connecting the two ABDs also confers some propensity to loosely bundle F-actin. Drebrin's ABDs bind across multiple actin protomers and their subdomains and modify the longitudinal inter-protomer interface, explaining its F-actin stabilising properties. Furthermore, we show drebrin's binding site on F-actin is shared with other critical actin-binding and regulatory proteins, explaining their competitive displacement.

Structural mechanisms of drebrin-mediated F-actin network modulation.,Zhao W, Chu LY, Abis G, Oozeer F, Mulvaney T, Nagar N, Topf M, Gordon-Weeks PR, Conte MR, Atherton J Nat Commun. 2026 Jun 23;17(1):7894. doi: 10.1038/s41467-026-74543-6. PMID:42337253<ref>PMID:42337253</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9tga" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Abis G]]
[[Category: Atherton J]]
[[Category: Conte MR]]
[[Category: Gordon-Weeks PR]]
[[Category: Mulvaney T]]
[[Category: Nagar N]]
[[Category: Oozeer F]]
[[Category: Topf M]]
[[Category: Zhao W]]