8gn5

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'''Unreleased structure'''
 
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The entry 8gn5 is ON HOLD until 2025-02-23
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==Designed pH-responsive P22 VLP==
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<StructureSection load='8gn5' size='340' side='right'caption='[[8gn5]], [[Resolution|resolution]] 4.02&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8gn5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergvirus Lederbergvirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GN5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.02&#8491;</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=8gn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gn5 OCA], [https://pdbe.org/8gn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gn5 RCSB], [https://www.ebi.ac.uk/pdbsum/8gn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gn5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPSD_BPP22 CAPSD_BPP22] Assembles to form an icosahedral capsid with a T=7 symmetry.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A stimuli-responsive protein self-assembly offers promising utility as a protein nanocage for biotechnological and medical applications. Herein, the development of a virus-like particle (VLP) that undergoes a transition between assembly and disassembly under a neutral and acidic pH, respectively, for a targeted delivery is reported. The structure of the bacteriophage P22 coat protein is used for the computational design of coat subunits that self-assemble into a pH-responsive VLP. Subunit designs are generated through iterative computational cycles of histidine substitutions and evaluation of the interaction energies among the subunits under an acidic and neutral pH. The top subunit designs are tested and one that is assembled into a VLP showing the highest pH-dependent structural transition is selected. The cryo-EM structure of the VLP is determined, and the structural basis of a pH-triggered disassembly is delineated. The utility of the designed VLP is exemplified through the targeted delivery of a cytotoxic protein cargo into tumor cells in a pH-dependent manner. These results provide strategies for the development of self-assembling protein architectures with new functionality for diverse applications.
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Authors:
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A pH-Responsive Virus-Like Particle as a Protein Cage for a Targeted Delivery.,Kim KJ, Kim G, Bae JH, Song JJ, Kim HS Adv Healthc Mater. 2023 Nov 15:e2302656. doi: 10.1002/adhm.202302656. PMID:37966427<ref>PMID:37966427</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8gn5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Lederbergvirus]]
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[[Category: Bae JH]]
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[[Category: Kim G]]
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[[Category: Kim HS]]
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[[Category: Kim KJ]]
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[[Category: Song JJ]]

Revision as of 11:41, 1 February 2024

Designed pH-responsive P22 VLP

PDB ID 8gn5

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