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The | ==Structure of Hepatitis B Virus Capsid Y132A mutant in complex with Compound 24== | ||
<StructureSection load='8gih' size='340' side='right'caption='[[8gih]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8gih]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus Hepatitis B virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GIH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZMH:(6S,8R)-N-(3-bromo-4-fluorophenyl)-8-fluoro-10-methyl-11-oxo-1,3,4,7,8,9,10,11-octahydro-2H-pyrido[4,3 3,4]pyrazolo[1,5-a][1,4]diazepine-2-carboxamide'>ZMH</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=8gih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gih OCA], [https://pdbe.org/8gih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gih RCSB], [https://www.ebi.ac.uk/pdbsum/8gih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gih ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/L7R9I1_HBV L7R9I1_HBV] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The HBV capsid core protein serves a number of important functions in the viral life cycle enabling chronic HBV infection to persist, and therefore is a promising drug target. Interfering with capsid assembly has shown efficacy in clinical trials with small molecule capsid assembly modulators (CAMs). Herein is described the further optimization of a progressive series of diazepinone HBV CAMs. | |||
Diazepinone HBV capsid assembly modulators.,Kuduk SD, DeRatt LG, Stoops B, Shaffer P, Lam AM, Espiritu C, Vogel R, Lau V, Flores OA, Hartman GD Bioorg Med Chem Lett. 2022 Sep 15;72:128823. doi: 10.1016/j.bmcl.2022.128823. , Epub 2022 May 27. PMID:35644301<ref>PMID:35644301</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Shaffer | <div class="pdbe-citations 8gih" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hepatitis B virus]] | |||
[[Category: Large Structures]] | |||
[[Category: Shaffer PL]] | |||
Revision as of 23:34, 12 April 2023
Structure of Hepatitis B Virus Capsid Y132A mutant in complex with Compound 24Structure of Hepatitis B Virus Capsid Y132A mutant in complex with Compound 24
Structural highlights
FunctionPublication Abstract from PubMedThe HBV capsid core protein serves a number of important functions in the viral life cycle enabling chronic HBV infection to persist, and therefore is a promising drug target. Interfering with capsid assembly has shown efficacy in clinical trials with small molecule capsid assembly modulators (CAMs). Herein is described the further optimization of a progressive series of diazepinone HBV CAMs. Diazepinone HBV capsid assembly modulators.,Kuduk SD, DeRatt LG, Stoops B, Shaffer P, Lam AM, Espiritu C, Vogel R, Lau V, Flores OA, Hartman GD Bioorg Med Chem Lett. 2022 Sep 15;72:128823. doi: 10.1016/j.bmcl.2022.128823. , Epub 2022 May 27. PMID:35644301[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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