How binding of small molecule and peptide ligands to HIV-1 TAR alters the RNA motional landscape.

ABSTRACT: The HIV-1 TAR RNA represents a well-known paradigm to study the role of dynamics and conformational change in RNA function. This regulatory RNA changes conformation in response to binding of Tat protein and of a variety of peptidic and small molecule ligands, indicating that its conformational flexibility and intrinsic dynamics play important roles in molecular recognition. We have used (13)C NMR relaxation experiments to examine changes in the motional landscape of HIV-1 TAR in the presence of three ligands of different affinity and specificity. The ligands are argininamide, a linear peptide mimic of the Tat basic domain and a cyclic peptide that potently inhibits Tat-dependent activation of transcription. All three molecules induce the same motional characteristics within the three nucle

SUBMITTER: Bardaro MF 

PROVIDER: S-EPMC2655691 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature