1MNB

BIV TAT PEPTIDE (RESIDUES 68-81), NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1MNB

• Entry DOI: 10.2210/pdb1mnb/pdb
• Descriptor: BIV TAR RNA, BIV TAT PEPTIDE (2 entities in total)
• Functional Keywords: complex (regulatory protein-rna), transcription regulation, viral protein-rna complex, viral protein/rna
• Cellular location: Host nucleus, host nucleolus: P19564
• Total number of polymer chains: 2
• Total formula weight: 10653.39

Authors

Puglisi, J.D.,Chen, L.,Blanchard, S.,Frankel, A.D. (deposition date: 1996-07-25, release date: 1997-01-27, Last modification date: 2024-05-22)

Primary citation

Puglisi, J.D.,Chen, L.,Blanchard, S.,Frankel, A.D.
Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex.
Science, 270:1200-1203, 1995

PubMed Abstract: The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.

PubMed: 7502045

Experimental method

SOLUTION NMR