Oligopeptide inhibition of class I ribonucleotide reductases
Identifieur interne : 001C16 ( Istex/Corpus ); précédent : 001C15; suivant : 001C17Oligopeptide inhibition of class I ribonucleotide reductases
Auteurs : Barry S. CoopermanSource :
- Peptide Science [ 0006-3525 ] ; 2003.
Abstract
Class I ribonucleotide reductases (RRs), which are well‐recognized targets for cancer chemotherapeutic and antiviral agents, are composed of two different subunits, R1 and R2, and are inhibited by oligopeptides corresponding to the C‐terminus of R2, which compete with R2 for binding to R1. These peptides specifically inhibit the RRs from which they are derived, and closely homologous RRs, but do not inhibit less homologous RRs. Here we review results obtained for oligopeptide inhibition of RRs from several sources, including related x‐ray, NMR, and modeling results. The most extensive studies have been performed on herpes simplex virus‐RR (HSV‐RR) and mammalian‐RR (mRR). A common model fits the data obtained for both enzymes, in which the C‐terminal residue of the oligopeptide (Leu for HSV‐RR, Phe for mRR) binds with high specificity to a narrow and deep hydrophobic subsite, and two or more hydrophobic groups at the N‐terminal portion of the peptide bind to a broad and shallow second hydrophobic subsite. The studies have led to the development of highly potent and specific inhibitors of HSV‐RR and promising inhibitors of mRR, and indicate possible directions for the development of inhibitors of bacterial and fungal RRs. © 2003 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 71: 117–131, 2003
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DOI: 10.1002/bip.10397
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These peptides specifically inhibit the RRs from which they are derived, and closely homologous RRs, but do not inhibit less homologous RRs. Here we review results obtained for oligopeptide inhibition of RRs from several sources, including related x‐ray, NMR, and modeling results. The most extensive studies have been performed on herpes simplex virus‐RR (HSV‐RR) and mammalian‐RR (mRR). A common model fits the data obtained for both enzymes, in which the C‐terminal residue of the oligopeptide (Leu for HSV‐RR, Phe for mRR) binds with high specificity to a narrow and deep hydrophobic subsite, and two or more hydrophobic groups at the N‐terminal portion of the peptide bind to a broad and shallow second hydrophobic subsite. The studies have led to the development of highly potent and specific inhibitors of HSV‐RR and promising inhibitors of mRR, and indicate possible directions for the development of inhibitors of bacterial and fungal RRs. © 2003 Wiley Periodicals, Inc. 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xml:id="kwd2">oligopeptide inhibitor</keyword><keyword xml:id="kwd3">chemotherapy</keyword><keyword xml:id="kwd4">antiviral</keyword><keyword xml:id="kwd5">transfer nuclear Overhauser effect</keyword><keyword xml:id="kwd6">modeling</keyword><keyword xml:id="kwd7">allosteric regulation</keyword><keyword xml:id="kwd8">species specificity</keyword></keywordGroup><fundingInfo><fundingAgency>NIH</fundingAgency><fundingNumber>CA58567</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Class I ribonucleotide reductases (RRs), which are well‐recognized targets for cancer chemotherapeutic and antiviral agents, are composed of two different subunits, R1 and R2, and are inhibited by oligopeptides corresponding to the C‐terminus of R2, which compete with R2 for binding to R1. These peptides specifically inhibit the RRs from which they are derived, and closely homologous RRs, but do not inhibit less homologous RRs. Here we review results obtained for oligopeptide inhibition of RRs from several sources, including related x‐ray, NMR, and modeling results. The most extensive studies have been performed on herpes simplex virus‐RR (HSV‐RR) and mammalian‐RR (mRR). A common model fits the data obtained for both enzymes, in which the C‐terminal residue of the oligopeptide (Leu for HSV‐RR, Phe for mRR) binds with high specificity to a narrow and deep hydrophobic subsite, and two or more hydrophobic groups at the N‐terminal portion of the peptide bind to a broad and shallow second hydrophobic subsite. The studies have led to the development of highly potent and specific inhibitors of HSV‐RR and promising inhibitors of mRR, and indicate possible directions for the development of inhibitors of bacterial and fungal RRs. © 2003 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 71: 117–131, 2003</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Oligopeptide inhibition of class I ribonucleotide reductases</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Oligopeptide Inhibition</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Oligopeptide inhibition of class I ribonucleotide reductases</title></titleInfo><name type="personal"><namePart type="given">Barry S.</namePart><namePart type="family">Cooperman</namePart><affiliation>Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104‐6323</affiliation><affiliation>E-mail: cooprman@pobox.upenn.edu</affiliation><affiliation>Correspondence address: Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104‐6323</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2003</dateIssued><copyrightDate encoding="w3cdtf">2003</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">9</extent><extent unit="tables">4</extent><extent unit="references">77</extent><extent unit="words">7961</extent></physicalDescription><abstract lang="en">Class I ribonucleotide reductases (RRs), which are well‐recognized targets for cancer chemotherapeutic and antiviral agents, are composed of two different subunits, R1 and R2, and are inhibited by oligopeptides corresponding to the C‐terminus of R2, which compete with R2 for binding to R1. These peptides specifically inhibit the RRs from which they are derived, and closely homologous RRs, but do not inhibit less homologous RRs. Here we review results obtained for oligopeptide inhibition of RRs from several sources, including related x‐ray, NMR, and modeling results. The most extensive studies have been performed on herpes simplex virus‐RR (HSV‐RR) and mammalian‐RR (mRR). A common model fits the data obtained for both enzymes, in which the C‐terminal residue of the oligopeptide (Leu for HSV‐RR, Phe for mRR) binds with high specificity to a narrow and deep hydrophobic subsite, and two or more hydrophobic groups at the N‐terminal portion of the peptide bind to a broad and shallow second hydrophobic subsite. The studies have led to the development of highly potent and specific inhibitors of HSV‐RR and promising inhibitors of mRR, and indicate possible directions for the development of inhibitors of bacterial and fungal RRs. © 2003 Wiley Periodicals, Inc. 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