8cdt: Difference between revisions
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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=8cdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cdt OCA], [https://pdbe.org/8cdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cdt RCSB], [https://www.ebi.ac.uk/pdbsum/8cdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cdt ProSAT]</span></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=8cdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cdt OCA], [https://pdbe.org/8cdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cdt RCSB], [https://www.ebi.ac.uk/pdbsum/8cdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cdt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nuclear pore complex (NPC) biogenesis is a still enigmatic example of protein self-assembly. We now introduce several cross-reacting anti-Nup nanobodies for imaging intact nuclear pore complexes from frog to human. We also report a simplified assay that directly tracks postmitotic NPC assembly with added fluorophore-labeled anti-Nup nanobodies. During interphase, NPCs are inserted into a pre-existing nuclear envelope. Monitoring this process is challenging because newly assembled NPCs are indistinguishable from pre-existing ones. We overcame this problem by inserting Xenopus-derived NPCs into human nuclear envelopes and using frog-specific anti-Nup nanobodies for detection. We further asked whether anti-Nup nanobodies could serve as NPC assembly inhibitors. Using a selection strategy against conserved epitopes, we obtained anti-Nup93, Nup98, and Nup155 nanobodies that block Nup-Nup interfaces and arrest NPC assembly. We solved structures of nanobody-target complexes and identified roles for the Nup93 alpha-solenoid domain in recruiting Nup358 and the Nup214.88.62 complex, as well as for Nup155 and the Nup98 autoproteolytic domain in NPC scaffold assembly. The latter suggests a checkpoint linking pore formation to the assembly of the Nup98-dominated permeability barrier. | |||
A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies.,Sola Colom M, Fu Z, Gunkel P, Guttler T, Trakhanov S, Srinivasan V, Gregor K, Pleiner T, Gorlich D EMBO J. 2024 Jun;43(11):2198-2232. doi: 10.1038/s44318-024-00081-w. Epub 2024 Apr , 22. PMID:38649536<ref>PMID:38649536</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8cdt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 08:17, 12 June 2024
Crystal structure of the xNup93-Nb2t VHH antibodyCrystal structure of the xNup93-Nb2t VHH antibody
Structural highlights
Publication Abstract from PubMedNuclear pore complex (NPC) biogenesis is a still enigmatic example of protein self-assembly. We now introduce several cross-reacting anti-Nup nanobodies for imaging intact nuclear pore complexes from frog to human. We also report a simplified assay that directly tracks postmitotic NPC assembly with added fluorophore-labeled anti-Nup nanobodies. During interphase, NPCs are inserted into a pre-existing nuclear envelope. Monitoring this process is challenging because newly assembled NPCs are indistinguishable from pre-existing ones. We overcame this problem by inserting Xenopus-derived NPCs into human nuclear envelopes and using frog-specific anti-Nup nanobodies for detection. We further asked whether anti-Nup nanobodies could serve as NPC assembly inhibitors. Using a selection strategy against conserved epitopes, we obtained anti-Nup93, Nup98, and Nup155 nanobodies that block Nup-Nup interfaces and arrest NPC assembly. We solved structures of nanobody-target complexes and identified roles for the Nup93 alpha-solenoid domain in recruiting Nup358 and the Nup214.88.62 complex, as well as for Nup155 and the Nup98 autoproteolytic domain in NPC scaffold assembly. The latter suggests a checkpoint linking pore formation to the assembly of the Nup98-dominated permeability barrier. A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies.,Sola Colom M, Fu Z, Gunkel P, Guttler T, Trakhanov S, Srinivasan V, Gregor K, Pleiner T, Gorlich D EMBO J. 2024 Jun;43(11):2198-2232. doi: 10.1038/s44318-024-00081-w. Epub 2024 Apr , 22. PMID:38649536[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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