1njt

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(New page: 200px<br /><applet load="1njt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1njt, resolution 2.50&Aring;" /> '''COMPLEX STRUCTURE OF...)
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[[Image:1njt.gif|left|200px]]<br /><applet load="1njt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1njt, resolution 2.50&Aring;" />
 
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'''COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR'''<br />
 
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==Overview==
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==COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR==
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Herpesvirus protease is required for the life cycle of the virus and is an, attractive target for the design and development of new anti-herpes, agents. The protease belongs to a new class of serine proteases, with a, novel backbone fold and a unique Ser-His-His catalytic triad. Here we, report the crystal structures of human cytomegalovirus protease in complex, with two peptidomimetic inhibitors. The structures reveal a new, hydrogen-bonding interaction between the main chain carbonyl of the P(5), residue and the main chain amide of amino acid 137 of the protease, which, is important for the binding affinity of the inhibitor. Conformational, flexibility was observed in the S(3) pocket of the enzyme, and this is, supported by our characterization of several mutants in this pocket. One, of the structures is at 2.5 A resolution, allowing us for the first time, to locate ordered solvent molecules in the inhibitor complex. The presence, of two solvent molecules in the active site may have implications for the, design of new inhibitors against this enzyme. Favorable and stereospecific, interactions have been established in the S(1)' pocket for one of these, inhibitors.
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<StructureSection load='1njt' size='340' side='right'caption='[[1njt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1njt]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NJT 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">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CFT:TRIFLUOROMETHANE'>CFT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMH:N4,N4-DIMETHYL-ASPARAGINE'>DMH</scene>, <scene name='pdbligand=DMK:3,3-DIMETHYL+ASPARTIC+ACID'>DMK</scene></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=1njt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1njt OCA], [https://pdbe.org/1njt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1njt RCSB], [https://www.ebi.ac.uk/pdbsum/1njt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1njt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/1njt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1njt ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1NJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5] with CL, ACE and CFT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NJT OCA].
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*[[Virus protease 3D structures|Virus protease 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural and biochemical studies of inhibitor binding to human cytomegalovirus protease., Khayat R, Batra R, Qian C, Halmos T, Bailey M, Tong L, Biochemistry. 2003 Feb 4;42(4):885-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12549906 12549906]
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[[Category: Human betaherpesvirus 5]]
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[[Category: Assemblin]]
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[[Category: Large Structures]]
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[[Category: Human herpesvirus 5]]
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[[Category: Bailey M]]
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[[Category: Single protein]]
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[[Category: Batra R]]
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[[Category: Bailey, M.]]
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[[Category: Halmos T]]
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[[Category: Batra, R.]]
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[[Category: Khayat R]]
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[[Category: Halmos, T.]]
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[[Category: Qian C]]
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[[Category: Khayat, R.]]
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[[Category: Tong L]]
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[[Category: Qian, C.]]
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[[Category: Tong, L.]]
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[[Category: ACE]]
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[[Category: CFT]]
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[[Category: CL]]
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[[Category: hydrolase]]
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[[Category: induced-fit]]
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[[Category: peptidomimetic inhibitor]]
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[[Category: protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:19:41 2007''
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Current revision

COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR

PDB ID 1njt

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