View source for 7fdj


==Engineered Hepatitis B virus core antigen with short linker T=4==
<StructureSection load='7fdj' size='340' side='right'caption='[[7fdj]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FDJ 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]] 4.4&#8491;</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=7fdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fdj OCA], [https://pdbe.org/7fdj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fdj RCSB], [https://www.ebi.ac.uk/pdbsum/7fdj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fdj ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Cancer targeting nanoparticles have been extensively studied, but stable and applicable agents have yet to be developed. Here, we report stable nanoparticles based on hepatitis B core antigen (HBcAg) for cancer therapy. HBcAg monomers assemble into spherical capsids of 180 or 240 subunits. HBcAg was engineered to present an affibody for binding to human epidermal growth factor receptor 1 (EGFR) and to present histidine and tyrosine tags for binding to gold ions. The HBcAg engineered to present affibody and tags (HAF) bound specifically to EGFR and exterminated the EGFR-overexpressing adenocarcinomas under alternating magnetic field (AMF) after binding with gold ions. Using cryogenic electron microscopy (cryo-EM), we obtained the molecular structures of recombinant HAF and found that the overall structure of HAF was the same as that of HBcAg, except with the affibody on the spike. Therefore, HAF is viable for cancer therapy with the advantage of maintaining a stable capsid form. If the affibody in HAF is replaced with a specific sequence to bind to another targetable disease protein, the nanoparticles can be used for drug development over a wide spectrum.

Structural and Functional Characterizations of Cancer Targeting Nanoparticles Based on Hepatitis B Virus Capsid.,Heo Y, Jeong H, Yoo Y, Yun JH, Ryu B, Cha YJ, Lee BR, Jeon YE, Kim J, Jeong S, Jo E, Woo JS, Lee J, Cho HS, Lee W Int J Mol Sci. 2021 Aug 24;22(17). pii: ijms22179140. doi: 10.3390/ijms22179140. PMID:34502049<ref>PMID:34502049</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cho H]]
[[Category: Heo Y]]
[[Category: Jeong H]]
[[Category: Lee W]]
[[Category: Ryu B]]
[[Category: Yoo Y]]
[[Category: Yun J]]