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Literature summary for 3.1.26.13 extracted from

  • Temiz, N.; Bahar, I.
    Inhibitor binding alters the directions of domain motions in HIV-1 reverse transcriptase (2002), Proteins Struct. Funct. Genet., 49, 61-70.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
study on dynamics of RT in unliganded and inhibitor-bound forms by structure-based approach. Non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities. The second generation non-nucleoside reverse transcriptase inhibitor, efavirenz, on the other hand, shows the stronger effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations. A second hinge site controlling the global rotational reorientations of the RNase H domain is identified Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
efavirenz second generation non-nucleoside reverse transcriptase inhibitor, shows the effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations Human immunodeficiency virus 1
nevirapine non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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