1fl1: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fl1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FL1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fl1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FL1 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1at3|1at3]], [[1vzv|1vzv]], [[1cmv|1cmv]], [[1wpo|1wpo]], [[1lay|1lay]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1at3|1at3]], [[1vzv|1vzv]], [[1cmv|1cmv]], [[1wpo|1wpo]], [[1lay|1lay]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fl1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fl1 RCSB], [http://www.ebi.ac.uk/pdbsum/1fl1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fl1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fl1 RCSB], [http://www.ebi.ac.uk/pdbsum/1fl1 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human herpesvirus 8]] | [[Category: Human herpesvirus 8]] | ||
[[Category: Craik, C S | [[Category: Craik, C S]] | ||
[[Category: Pray, T R | [[Category: Pray, T R]] | ||
[[Category: Reiling, K K | [[Category: Reiling, K K]] | ||
[[Category: Stroud, R M | [[Category: Stroud, R M]] | ||
[[Category: Antiviral drug design]] | [[Category: Antiviral drug design]] | ||
[[Category: Assemblin]] | [[Category: Assemblin]] | ||
Revision as of 00:59, 23 December 2014
KSHV PROTEASEKSHV PROTEASE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr), at 2.2 A resolution, reveals the active-site geometry and defines multiple possible target sites for drug design against a human cancer-producing virus. The catalytic triad of KSHV Pr, (Ser114, His46, and His157) and transition-state stabilization site are arranged as in other structurally characterized herpesviral proteases. The distal histidine-histidine hydrogen bond is solvent accessible, unlike the situation in other classes of serine proteases. As in all herpesviral proteases, the enzyme is active only as a weakly associated dimer (K(d) approximately 2 microM), and inactive as a monomer. Therefore, both the active site and dimer interface are potential targets for antiviral drug design. The dimer interface in KSHV Pr is compared with the interface of other herpesviral proteases. Two conserved arginines (Arg209), one from each monomer, are buried within the same region of the dimer interface. We propose that this conserved arginine may provide a destabilizing element contributing to the tuned micromolar dissociation of herpesviral protease dimers. Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements.,Reiling KK, Pray TR, Craik CS, Stroud RM Biochemistry. 2000 Oct 24;39(42):12796-803. PMID:11041844[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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