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1BIV

BOVINE IMMUNODEFICIENCY VIRUS TAT-TAR COMPLEX, NMR, 5 STRUCTURES

Summary for 1BIV
Entry DOI10.2210/pdb1biv/pdb
DescriptorTAR RNA, TAT PEPTIDE (2 entities in total)
Functional Keywordstat-tar, arg-gua interactions, buttressing u(dot)au base triple, glycine and isoleucine packing, peptide rna recognition, rna bending, complex (ribonucleic acid-peptide), viral protein-rna complex, viral protein/rna
Biological sourcesynthetic construct
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Total number of polymer chains2
Total formula weight10894.64
Authors
Ye, X.,Kumar, R.A.,Patel, D.J. (deposition date: 1996-06-12, release date: 1996-12-23, Last modification date: 2024-04-10)
Primary citationYe, X.,Kumar, R.A.,Patel, D.J.
Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex.
Chem.Biol., 2:827-840, 1995
Cited by
PubMed Abstract: In lentiviruses such as human immunodeficiency virus (HIV) and bovine immunodeficiency virus (BIV), the Tat (trans-activating) protein enhances transcription of the viral RNA by complexing to the 5'-end of the transcribed mRNA, at a region known as TAR (the trans-activation response element). Identification of the determinants that account for specific molecular recognition requires a high resolution structure of the Tat peptide-TAR RNA complex.
PubMed: 8807816
DOI: 10.1016/1074-5521(95)90089-6
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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