View source for 8skn


==Crystal structure of compound 3-bound human Dynamin-1-like protein GTPase-BSE fusion==
<StructureSection load='8skn' size='340' side='right'caption='[[8skn]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8skn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SKN 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]] 2.41&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6I9:N-[4-(azetidin-1-yl)-2-(4-methylphenyl)quinolin-6-yl]-2-methylpropanamide'>6I9</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=8skn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8skn OCA], [https://pdbe.org/8skn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8skn RCSB], [https://www.ebi.ac.uk/pdbsum/8skn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8skn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D3DUW7_HUMAN D3DUW7_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mitochondrial dysfunction has been attributed to many disease indications, including metabolic, cardiovascular, neoplastic, and neurodegenerative diseases. Dynamin related protein 1 (DRP1) is crucial in regulating mitochondrial fission and maintaining mitochondrial homeostasis. MiD49 is a dynamic peripheral protein receptor on the surface of the mitochondrial membrane that recruits DRP1 protein to induce mitochondrial binary fission. By targeting the protein-protein interaction of DRP1/MiD49, we have discovered a novel and potent allosteric DRP1 inhibitor that inhibits mitochondria fragmentation in vitro. X-ray cocrystal structure revealed that it locked the closed DRP1 conformation by induced dimerization.

Discovery of Potent Allosteric DRP1 Inhibitors by Disrupting Protein-Protein Interaction with MiD49.,Furuya T, Lin J, Afanaseva A, Molz L, Lagu B, Ma B ACS Med Chem Lett. 2023 Jul 24;14(8):1095-1099. doi: , 10.1021/acsmedchemlett.3c00223. eCollection 2023 Aug 10. PMID:37583827<ref>PMID:37583827</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8skn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ma B]]