View source for 1bfz


==BOUND CONFORMATION OF N-TERMINAL CLEAVAGE PRODUCT PEPTIDE MIMIC (P1-P9 OF RELEASE SITE) WHILE BOUND TO HCMV PROTEASE AS DETERMINED BY TRANSFERRED NOESY EXPERIMENTS (P1-P5 SHOWN ONLY), NMR, 32 STRUCTURES==
<StructureSection load='1bfz' size='340' side='right'caption='[[1bfz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bfz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 32 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=1bfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfz OCA], [https://pdbe.org/1bfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfz RCSB], [https://www.ebi.ac.uk/pdbsum/1bfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfz ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Substrate hydrolysis by human cytomegalovirus (HCMV) protease is essential to viral capsid assembly. The interaction of HCMV protease and the N-terminal cleavage products of the hydrolysis of R- and M-site oligopeptide substrate mimics (R and M, respectively, which span the P9-P1 positions) was studied by NMR methods. Protease-induced differential line broadening indicated that ligand binding is mediated by the P4-P1 amino acid residues of the peptides. A well-defined extended conformation of R from P1 through P4 when complexed to HCMV protease was evidenced by numerous transferred nuclear Overhauser effect (NOE) correlations for the peptide upon addition of the enzyme. NOE cross-peaks between the P4 and P5 side chains placing these two groups in proximity indicated a deviation from the extended conformation starting at P5. Similar studies carried out for the M peptide also indicated an extended peptide structure very similar to that of R, although the conformation of the P5 glycine could not be established. No obvious variation in structure between bound R and M (notably at P4, where the tyrosine of the R-site has been suggested to play a key role in ligand binding) could be discerned that might explain the observed differences in processing rates between R- and M-sequences. Kinetic studies, utilizing R- and M-site peptide substrates for which the P5 and P4 residues were separately exchanged, revealed that these positions had essentially no influence on the specificity constants (kcat/KM). In sharp contrast, substitution of the P2 residue of an M-site peptide changed its specificity constant to that of an R-site peptide substrate, and vice versa.

Human cytomegalovirus protease complexes its substrate recognition sequences in an extended peptide conformation.,LaPlante SR, Aubry N, Bonneau PR, Cameron DR, Lagace L, Massariol MJ, Montpetit H, Plouffe C, Kawai SH, Fulton BD, Chen Z, Ni F Biochemistry. 1998 Jul 7;37(27):9793-801. PMID:9657693<ref>PMID:9657693</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bfz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Aubry N]]
[[Category: Bonneau PR]]
[[Category: Cameron DR]]
[[Category: Chen Z]]
[[Category: Fulton BD]]
[[Category: Kawai SH]]
[[Category: Lagace L]]
[[Category: Laplante SR]]
[[Category: Massariol M-J]]
[[Category: Montpetit H]]
[[Category: Ni F]]
[[Category: Ploufe C]]