Crystallization studies of the human immunodeficiency virus (HIV-1) Tat protein and its trans-activation response element (TAR) RNA.
Acta Crystallogr D Biol Crystallogr
; 50(Pt 4): 527-34, 1994 Jul 01.
Article
in En
| MEDLINE
| ID: mdl-15299414
ABSTRACT
Small single crystals are reported of a complex between a small peptide fragment of the HIV-1 Tat protein and a fragment of the RNA to which it binds. Tat is responsible for enhancing the level of expression of the human immunodeficiency virus type 1 (HIV-1) and is a logical target for AIDS therapy. Tat may function to increase the level of transcription initiation or to prevent premature termination of transcripts. In vitro, Tat binds through its basic domain (two Lys and six Arg in nine residues) to a three-nucleotide bulge of a stem-loop RNA structure called TAR. Complex formation between Tat and TAR is necessary for Tat activity. Peptides which contain the basic region of Tat also bind to TAR RNA. We have carried out crystallization experiments on a 27-nucleotide fragment of TAR RNA and on complexes between two Tat peptides and TAR.
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Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
1994
Document type:
Article
Affiliation country: