3njq

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Revision as of 10:00, 14 February 2024

Crystal structure of Kaposi's sarcoma-associated herpesvirus protease in complex with dimer disruptor

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Retrieved from "http://52.214.119.220/wiki/index.php/3njq"

Categories: Human herpesvirus 8 type M | Large Structures | Baharuddin A

@@ Line 3: / Line 3: @@
 <StructureSection load='3njq' size='340' side='right'caption='[[3njq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3njq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_8_type_m Human herpesvirus 8 type m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3njq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_8_type_M Human herpesvirus 8 type M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NJQ:3-BENZYL-4-({[6-(CYCLOHEXYLMETHYL)PYRIDIN-2-YL]CARBONYL}AMINO)BENZOIC+ACID'>NJQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NJQ:3-BENZYL-4-({[6-(CYCLOHEXYLMETHYL)PYRIDIN-2-YL]CARBONYL}AMINO)BENZOIC+ACID'>NJQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rhadinovirus ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=435895 Human herpesvirus 8 type M])</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=3njq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njq OCA], [https://pdbe.org/3njq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3njq RCSB], [https://www.ebi.ac.uk/pdbsum/3njq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3njq ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/P88911_HHV8 P88911_HHV8]
-All members of the human herpesvirus protease (HHV Pr) family are active as weakly associating dimers but inactive as monomers. A small-molecule allosteric inhibitor of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr) traps the enzyme in an inactive monomeric state where the C-terminal helices are unfolded and the hydrophobic dimer interface is exposed. NMR titration studies demonstrate that the inhibitor binds to KSHV Pr monomers with low micromolar affinity. A 2.0-A-resolution X-ray crystal structure of a C-terminal truncated KSHV Pr-inhibitor complex locates the binding pocket at the dimer interface and displays significant conformational perturbations at the active site, 15 A from the allosteric site. NMR and CD data suggest that the small molecule inhibits human cytomegalovirus protease via a similar mechanism. As all HHV Prs are functionally and structurally homologous, the inhibitor represents a class of compounds that may be developed into broad-spectrum therapeutics that allosterically regulate enzymatic activity by disrupting protein-protein interactions.
-Enzyme inhibition by allosteric capture of an inactive conformation.,Lee GM, Shahian T, Baharuddin A, Gable JE, Craik CS J Mol Biol. 2011 Sep 2;411(5):999-1016. Epub 2011 Jun 22. PMID:21723875<ref>PMID:21723875</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3njq" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Virus protease 3D structures|Virus protease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human herpesvirus 8 type m]]
+[[Category: Human herpesvirus 8 type M]]
 [[Category: Large Structures]]
-[[Category: Baharuddin, A]]
+[[Category: Baharuddin A]]
-[[Category: Herpesvirus protease]]
-[[Category: Kshv]]
-[[Category: Kshv protease]]
-[[Category: Protein-dimer disruptor complex]]
-[[Category: Viral protein-inhibitor complex]]

3njq

From Proteopedia

Revision as of 10:00, 14 February 2024

Crystal structure of Kaposi's sarcoma-associated herpesvirus protease in complex with dimer disruptor

Structural highlights

Function

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

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