1bfz

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[[Image:1bfz.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1bfz| PDB=1bfz | SCENE= }}
{{STRUCTURE_1bfz| PDB=1bfz | SCENE= }}
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'''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'''
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===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===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_9657693}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9657693 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9657693}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFZ OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFZ OCA].
==Reference==
==Reference==
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[[Category: Substrate]]
[[Category: Substrate]]
[[Category: Transferred noesy]]
[[Category: Transferred noesy]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:27:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:04:32 2008''

Revision as of 16:04, 30 June 2008

Image:1bfz.png

Template:STRUCTURE 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

Template:ABSTRACT PUBMED 9657693

About this Structure

Full experimental information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jun 30 19:04:32 2008

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