1JM4: NMR Structure of P/CAF Bromodomain in Complex with HIV-1 Tat Peptide

The human immunodeficiency virus type 1 (HIV-1) trans-activator protein Tat stimulates transcription of the integrated HIV-1 genome and promotes viral replication in infected cells. Tat transactivation activity is dependent on lysine acetylation and its association with nuclear histone acetyltransferases p300/CBP (CREB binding protein) and p300/CBP-associated factor (PCAF). Here, we show that the bromodomain of PCAF binds specifically to HIV-1 Tat acetylated at lysine 50 and that this interaction competes effectively against HIV-1 TAR RNA binding to the lysine-acetylated Tat. The three-dimensional solution structure of the PCAF bromodomain in complex with a lysine 50-acetylated Tat peptide together with biochemical analyses provides the structural basis for the specificity of this molecular recognition and reveals insights into the differences in ligand selectivity of bromodomains.
PDB ID: 1JM4Download
MMDB ID: 162365
PDB Deposition Date: 2001/7/17
Updated in MMDB: 2018/05
Experimental Method:
solution nmr
Source Organism:
Homo sapiens
Similar Structures:
Molecular Components in 1JM4
Label Count Molecule
Proteins (2 molecules)
Hiv-1 TAT Peptide
Molecule annotation
P300/cbp-associated Factor(Gene symbol: KAT2B)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB