| The retroviral enzymes. | |
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MedLine Citation:
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PMID: 7526778 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have reviewed the current state of knowledge concerning the three enzymes common to all retroviruses. It is informative to consider them together, since their activities are interrelated. The enzymatic activities of RT and IN depend on processing of polyprotein precursors by PR. Furthermore, RT produces the viral DNA substrate to be acted upon by IN. All three of these retroviral enzymes function as multimers, and it is conceivable that specific polyprotein precursor interactions facilitate the multimerization of all of them. The multimeric structures of the enzymes are, however, quite different. PR is a symmetric homodimer whose subunits contribute to formation of a single active site. RT (of HIV, at least) is an asymmetric heterodimer in which one subunit appears to contribute all of the catalytic activity and the second is catalytically inactive, but structurally important. IN also functions minimally as a dimer for processing and joining. The retroviral enzymes represent important targets for antiviral therapy. Considerable effort continues to be focused on developing PR and RT inhibitors. As more is learned about IN, such efforts can be extended. Since these enzymes are critical at different stages in the retroviral life cycle, one optimistic hope is that a combination of drugs that target all of them may be maximally effective as therapy for AIDS. |
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Authors:
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R A Katz; A M Skalka |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: Annual review of biochemistry Volume: 63 ISSN: 0066-4154 ISO Abbreviation: Annu. Rev. Biochem. Publication Date: 1994 |
Date Detail:
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Created Date: 1994-12-12 Completed Date: 1994-12-12 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985150R Medline TA: Annu Rev Biochem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 133-73 Citation Subset: IM; X |
Affiliation:
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Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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DNA Nucleotidyltransferases
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physiology* Endopeptidases / physiology* HIV Protease / physiology HIV Reverse Transcriptase Humans Integrases RNA-Directed DNA Polymerase / physiology* Retroviridae / enzymology* Virus Integration |
| Grant Support | |
ID/Acronym/Agency:
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CA06927/CA/NCI NIH HHS; CA47486/CA/NCI NIH HHS; RR05539/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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EC 2.7.7.-/DNA Nucleotidyltransferases; EC 2.7.7.-/Integrases; EC 2.7.7.49/HIV Reverse Transcriptase; EC 2.7.7.49/RNA-Directed DNA Polymerase; EC 3.4.-/Endopeptidases; EC 3.4.23.-/HIV Protease |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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