Dr. Dmitri Ivanov's lab looks at how physical interactions at
protein interfaces determine biological outcomes. Inhibition of protein-protein interactions remains one of the major challenges and opportunities of modern molecular pharmacology.
One of the goals of our studies is to identify critical contacts on protein interfaces that could potentially be blocked for therapeutic purposes. We are particularly
interested in the assembly of higher-order macromolecular structures
such as viral shells or multi-subunit cellular machines. We have developed novel drug-discovery strategies that combine NMR spectroscopy,
computational methods and chemical biology tools.
Yang Y, Brandariz-NuÃ±ez A, Fricke T, Ivanov DN, Sarnak Z, Diaz-Griffero F. Binding of the rhesus TRIM5Î± PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction. Virology. 2014 Jan 5;448:217-28.
Brandariz-NuÃ±ez A, Valle-Casuso JC, White TE, Nguyen L, Bhattacharya A,
Wang Z, Demeler B, Amie S, Knowlton C, Kim B, Ivanov DN, Diaz-Griffero
F. Contribution of oligomerization to the anti-HIV-1 properties of SAMHD1. Retrovirology. 2013 Nov 12;10:131.
Biris N, Tomashevski A, Bhattacharya A, Diaz-Griffero F, Ivanov DN. Rhesus monkey TRIM5Î± SPRY domain recognizes multiple epitopes that span several capsid monomers on the surface of the HIV-1 mature viral core. J Mol Biol. 2013 Dec 13;425(24):5032-44.
Brandariz-NuÃ±ez A, Roa A, Valle-Casuso JC, Biris N, Ivanov D, Diaz-Griffero F. Contribution of SUMO-interacting motifs and SUMOylation to the antiretroviral properties of TRIM5Î±. Virology. 2013 Jan 20;435(2):463-71.
Biris N, Yang Y, Taylor AB, Tomashevski A, Guo M, Hart PJ, Diaz-Griffero F, Ivanov DN. Structure of the rhesus monkey TRIM5Î± PRYSPRY domain, the HIV capsid recognition module.Proc Natl Acad Sci U S A. 2012 Aug 14;109(33):13278-83.