9mj4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Yeast V-ATPase Vo proton channel bound to nanobody 2WVA149== | |
| + | <StructureSection load='9mj4' size='340' side='right'caption='[[9mj4]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9mj4]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MJ4 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]] 3.7Å</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=9mj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mj4 OCA], [https://pdbe.org/9mj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mj4 RCSB], [https://www.ebi.ac.uk/pdbsum/9mj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mj4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VATL2_YEAST VATL2_YEAST] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:1837023</ref> <ref>PMID:9030535</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The vacuolar ATPase (V-ATPase; V(1)V(o)) is a multi-subunit rotary nanomotor proton pump that acidifies organelles in virtually all eukaryotic cells, and extracellular spaces in some specialized tissues of higher organisms. Evidence suggests that metastatic breast cancers mislocalize V-ATPase to the plasma membrane to promote cell survival and facilitate metastasis, making the V-ATPase a potential drug target. We have generated a library of camelid single-domain antibodies (Nanobodies; Nbs) against lipid-nanodisc reconstituted yeast V-ATPase V(o) proton channel subcomplex. Here, we present an in-depth characterization of three anti-V(o) Nbs using biochemical and biophysical in vitro experiments. We find that the Nbs bind V(o) with high affinity, with one Nb inhibiting holoenzyme activity and another one preventing enzyme assembly. Using cryoEM, we find that two of the Nbs bind the c subunit ring of the V(o) on the lumen side of the complex. Additionally, we show that one of the Nbs raised against yeast V(o) can pull down human V-ATPase (HsV(1)V(o)). Our research demonstrates Nb versatility to target and modulate the activity of the V-ATPase, and highlights the potential for future therapeutic Nb development. | ||
| - | + | Monoclonal nanobodies alter the activity and assembly of the yeast vacuolar H(+)-ATPase.,Knight K, Park JB, Oot RA, Khan MM, Roh SH, Wilkens S bioRxiv [Preprint]. 2025 Jan 11:2025.01.10.632502. doi: , 10.1101/2025.01.10.632502. PMID:39829782<ref>PMID:39829782</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9mj4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lama glama]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Knight K]] | ||
| + | [[Category: Wilkens S]] | ||
Current revision
Yeast V-ATPase Vo proton channel bound to nanobody 2WVA149
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