GTP activator and dNTP substrates of HIV-1 restriction factor SAMHD1 generate a long-lived activated state.

Hansen, Erik C; Seamon, Kyle J; Cravens, Shannen L; Stivers, James T

Hansen, Erik C; Seamon, Kyle J; Cravens, Shannen L; Stivers, James T.

Affiliation

Hansen EC; Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185.

Proc Natl Acad Sci U S A ; 111(18): E1843-51, 2014 May 06.

Article in En | MEDLINE | ID: mdl-24753578

Subject(s)

Deoxyribonucleotides/metabolism; Guanosine Triphosphate/metabolism; HIV-1/metabolism; Monomeric GTP-Binding Proteins/metabolism; Catalytic Domain; Deoxyguanine Nucleotides/metabolism; Deoxyguanosine/analogs & derivatives; Deoxyguanosine/metabolism; Deoxyuracil Nucleotides/metabolism; Enzyme Activation; HIV-1/immunology; HIV-1/pathogenicity; Humans; Immunity, Innate; Kinetics; Models, Molecular; Monomeric GTP-Binding Proteins/chemistry; Monomeric GTP-Binding Proteins/immunology; Protein Multimerization; Protein Structure, Quaternary; SAM Domain and HD Domain-Containing Protein 1; Substrate Specificity; Thionucleosides/metabolism

Key words

dNTP induced oligomerization; enzyme catalysis; innate immunity

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Full text: 1 Database: MEDLINE Main subject: HIV-1 / Monomeric GTP-Binding Proteins / Deoxyribonucleotides / Guanosine Triphosphate Type of study: Prognostic_studies Limits: Humans Language: En Year: 2014 Type: Article

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