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Backbone ¹H, ¹³C, and ¹?N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769.

ABSTRACT: HIV-1 protease (HIV-1PR) is an essential drug target in the treatment of patients infected with HIV-1. Mutations are found to arise in over 38 of 99 amino acid sites in this protein in response to drug therapy or natural selection, where many are found combinations that alter enzyme kinetics or inhibitor susceptibility without a clear structural mechanism. In efforts to understand how these mutations alter the flexibility and dynamics of HIV-1PR, we report the backbone (1)H, (13)C, and (15)N chemical shift assignments for subtypes C, circulating recombinant form CRF01_AE and a multi-drug resistant variant MDR 769. These assignments are essential for future work aimed at characterizing backbone dynamics, exchange dynamics and dynamics of protein/substrate or protein/inhibitor interactions.

SUBMITTER: Huang X

PROVIDER: S-EPMC3518686 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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Backbone ¹H, ¹³C, and ¹⁵N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769.

Huang Xi X de Vera Ian Mitchelle S IM Veloro Angelo M AM Rocca James R JR Simmerling Carlos C Dunn Ben M BM Fanucci Gail E GE

Biomolecular NMR assignments 20120701 2

HIV-1 protease (HIV-1PR) is an essential drug target in the treatment of patients infected with HIV-1. Mutations are found to arise in over 38 of 99 amino acid sites in this protein in response to drug therapy or natural selection, where many are found combinations that alter enzyme kinetics or inhibitor susceptibility without a clear structural mechanism. In efforts to understand how these mutations alter the flexibility and dynamics of HIV-1PR, we report the backbone (1)H, (13)C, and (15)N che ...[more]

PMID: 22752791

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