1JM4

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

Summary for 1JM4

• Entry DOI: 10.2210/pdb1jm4/pdb
• Related: 1B91
• NMR Information: BMRB: 4312
• Descriptor: HIV-1 Tat Peptide, P300/CBP-associated Factor (2 entities in total)
• Functional Keywords: bromodomain, protein-peptide complex, transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus (By similarity): Q92831
• Total number of polymer chains: 2
• Total formula weight: 15536.98

Authors

Mujtaba, S.,He, Y.,Zeng, L.,Farooq, A.,Carlson, J.E.,Ott, M.,Verdin, E.,Zhou, M.-M. (deposition date: 2001-07-17, release date: 2002-07-17, Last modification date: 2024-10-30)

Primary citation

Mujtaba, S.,He, Y.,Zeng, L.,Farooq, A.,Carlson, J.E.,Ott, M.,Verdin, E.,Zhou, M.-M.
Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain
Mol.Cell, 9:575-586, 2002

PubMed Abstract: 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.

PubMed: 11931765
DOI: 10.1016/S1097-2765(02)00483-5

Experimental method

SOLUTION NMR