2X7L

Implications of the HIV-1 Rev dimer structure at 3.2A resolution for multimeric binding to the Rev response element

Summary for 2X7L

• Entry DOI: 10.2210/pdb2x7l/pdb
• Descriptor: FAB HEAVY CHAIN, FAB LIGHT CHAIN, PROTEIN REV (3 entities in total)
• Functional Keywords: nuclear export, immune system, post-transcriptional regulation
• Biological source: synthetic construct; More
• Total number of polymer chains: 18
• Total formula weight: 365002.76

Authors

DiMattia, M.A.,Watts, N.R.,Stahl, S.J.,Rader, C.,Wingfield, P.T.,Stuart, D.I.,Steven, A.C.,Grimes, J.M. (deposition date: 2010-03-01, release date: 2010-03-23, Last modification date: 2023-12-20)

Primary citation

Dimattia, M.A.,Watts, N.R.,Stahl, S.J.,Rader, C.,Wingfield, P.T.,Stuart, D.I.,Steven, A.C.,Grimes, J.M.
Implications of the HIV-1 Rev Dimer Structure at 3. 2 A Resolution for Multimeric Binding to the Rev Response Element.
Proc.Natl.Acad.Sci.USA, 107:5810-, 2010

PubMed Abstract: HIV-1 Rev is a small regulatory protein that mediates the nuclear export of viral mRNAs, an essential step in the HIV replication cycle. In this process Rev oligomerizes in association with a highly structured RNA motif, the Rev response element. Crystallographic studies of Rev have been hampered by the protein's tendency to aggregate, but Rev has now been found to form a stable soluble equimolar complex with a specifically engineered monoclonal Fab fragment. We have determined the structure of this complex at 3.2 A resolution. It reveals a molecular dimer of Rev, bound on either side by a Fab, where the ordered portion of each Rev monomer (residues 9-65) contains two coplanar alpha-helices arranged in hairpin fashion. Subunits dimerize through overlapping of the hairpin prongs. Mating of hydrophobic patches on the outer surface of the dimer is likely to promote higher order interactions, suggesting a model for Rev oligomerization onto the viral RNA.

PubMed: 20231488
DOI: 10.1073/PNAS.0914946107

Experimental method

X-RAY DIFFRACTION (3.17 Å)