Conformational Changes in HIV-1 Reverse Transcriptase that Facilitate Its Maturation.

HIV Protease / metabolism HIV Reverse Transcriptase / chemistry HIV-1 / chemistry Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Multimerization Proteolysis RNA, Transfer, Lys / metabolism
HIV-1 NMR maturation reverse transcriptase structure

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
01 10 2019
Historique:
received: 13 02 2019
revised: 10 07 2019
accepted: 09 08 2019
pubmed: 1 9 2019
medline: 21 5 2020
entrez: 1 9 2019
Statut: ppublish

Résumé

HIV-1 reverse transcriptase (RT) is translated as part of the Gag-Pol polyprotein that is proteolytically processed by HIV-1 protease (PR) to finally become a mature heterodimer, composed of a p66 and a p66-derived 51-kDa subunit, p51. Our previous work suggested that tRNA

Identifiants

DOI: 10.1016/j.str.2019.08.004 PMID: 31471129 PMC: PMC6774901
pubmed: 31471129
pii: S0969-2126(19)30275-8
doi: 10.1016/j.str.2019.08.004
pmc: PMC6774901
mid: NIHMS1537712
pii:
doi:

Substances chimiques

RNA, Transfer, Lys 0
reverse transcriptase, Human immunodeficiency virus 1 EC 2.7.7.-
HIV Reverse Transcriptase EC 2.7.7.49
HIV Protease EC 3.4.23.-

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1581-1593.e3

Subventions

Organisme : NIGMS NIH HHS
ID : P50 GM082251
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM118012
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM068406
Pays : United States
Organisme : NIAID NIH HHS
ID : P50 AI150481
Pays : United States
Organisme : NIAID NIH HHS
ID : U54 AI150472
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM105401
Pays : United States
Organisme : NIGMS NIH HHS
ID : P01 GM109767
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI077424
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

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Auteurs

Ryan L Slack (RL)

Department of Structural Biology, University of Pittsburgh School of Medicine, Room 1037, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.

Tatiana V Ilina (TV)

Department of Structural Biology, University of Pittsburgh School of Medicine, Room 1037, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.

Zhaoyong Xi (Z)

Department of Structural Biology, University of Pittsburgh School of Medicine, Room 1037, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.

Nicholas S Giacobbi (NS)

Department of Medicine, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.

Gota Kawai (G)

Department of Life and Environmental Sciences, Chiba Institute of Technology, Chiba, Japan.

Michael A Parniak (MA)

Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15219, USA.

Stefan G Sarafianos (SG)

Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, USA.

Nicolas Sluis Cremer (N)

Department of Medicine, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA. Electronic address: nps2@pitt.edu.

Rieko Ishima (R)

Department of Structural Biology, University of Pittsburgh School of Medicine, Room 1037, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA. Electronic address: ishima@pitt.edu.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales non structurales › Protéases virales › Protéase du VIH › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales structurales › Protéines nucléocapside › Protéines du core viral › Produits du gène pol › RNA-directed DNA polymerase › Transcriptase inverse du VIH › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Virus › Virus à ARN › Retroviridae › Lentivirus › Lentivirus des primates › VIH (Virus de l'Immunodéficience Humaine) › VIH-1 (Virus de l'Immunodéficience Humaine de type 1) › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Analyse spectrale › Spectroscopie par résonance magnétique › Résonance magnétique nucléaire biomoléculaire › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Multimérisation de protéines › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Métabolisme › Protéolyse › Conformational Changes in HIV-1 Reverse...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ARN › ARN de transfert › ARN de transfert spécifiques des différents acides aminés › ARN de transfert de la lysine › Conformational Changes in HIV-1 Reverse...