4zuh: Difference between revisions

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-'''Unreleased structure'''
-The entry 4zuh is ON HOLD  until Paper Publication
+==Complex structure of PEDV 3CLpro mutant (C144A) with a peptide substrate.==
+<StructureSection load='4zuh' size='340' side='right' caption='[[4zuh]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4zuh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZUH FirstGlance]. <br>
+</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=4zuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zuh OCA], [http://pdbe.org/4zuh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zuh RCSB], [http://www.ebi.ac.uk/pdbsum/4zuh PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Porcine epidemic diarrhea virus (PEDV), a member of the genus Alphacoronavirus, has caused significant damage to the Asian and American pork industries. Coronavirus 3C-like protease (3CL(pro)), which is involved in the processing of viral polyproteins for viral replication, is an appealing antiviral drug target. Here, we present the crystal structures of PEDV 3CL(pro) and a molecular complex between an inactive PEDV 3CL(pro) variant C144A bound to a peptide substrate. Structural characterization, mutagenesis and biochemical analysis reveal the substrate-binding pockets and the residues that comprise the active site of PEDV 3CL(pro). The dimerization of PEDV 3CL(pro) is similar to that of other Alphacoronavirus 3CL(pro)s but has several differences from that of SARS-CoV 3CL(pro) from the genus Betacoronavirus. Furthermore, the non-conserved motifs in the pockets cause different cleavage of substrate between PEDV and SARS-CoV 3CL(pro)s, which may provide new insights into the recognition of substrates by 3CL(pro)s in various coronavirus genera.
-Authors: Ye, G., Fu, Z.F., Peng, G.Q.
+Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease.,Ye G, Deng F, Shen Z, Luo R, Zhao L, Xiao S, Fu ZF, Peng G Virology. 2016 Jul;494:225-35. doi: 10.1016/j.virol.2016.04.018. Epub 2016 Apr, 26. PMID:27128350<ref>PMID:27128350</ref>
-Description: Complex structure of PEDV 3CLpro mutant (C144A) with a peptide substrate.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Peng, G.Q]]
+<div class="pdbe-citations 4zuh" style="background-color:#fffaf0;"></div>
-[[Category: Fu, Z.F]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Fu, Z F]]
+[[Category: Peng, G Q]]
 [[Category: Ye, G]]
+[[Category: 3c-like protease]]
+[[Category: Hydrolase-peptide complex]]