NMR structure of a biologically active peptide containing the RNA-binding domain of h
 

NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.

http://www.ncbi.nlm.nih.gov/corehtml...pubmed-pmc.gif Related Articles NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.

Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8248-52

Authors: Mujeeb A, Bishop K, Peterlin BM, Turck C, Parslow TG, James TL

The Tat protein of human immunodeficiency virus type 1 enhances transcription by binding to a specific RNA element on nascent viral transcripts. Binding is mediated by a 10-amino acid basic domain that is rich in arginines and lysines. Here we report the three-dimensional peptide backbone structure of a biologically active 25-mer peptide that contains the human immunodeficiency virus type 1 Tat basic domain linked to the core regulatory domain of another lentiviral Tat--i.e., that from equine infectious anemia virus. Circular dichroism and two-dimensional proton NMR studies of this hybrid peptide indicate that the Tat basic domain forms a stable alpha-helix, whereas the adjacent regulatory sequence is mostly in extended form. These findings suggest that the tendency to form stable alpha-helices may be a common property of arginine- and lysine-rich RNA-binding domains.

PMID: 8058789 [PubMed - indexed for MEDLINE]



Source: PubMed