Jerome and Lorraine Aresty Chair
Distinguished Professor
Department of Molecular Biology and Biochemistry
Rutgers–New Brunswick, School of Arts and Sciences

Adjunct Professor
Department of Biochemistry and Molecular Biology
RBHS, Robert Wood Johnson Medical School

Cancer Institute of New Jersey

Ph.D., 1987, Cornell University
Telephone: (848) 445-9866
Fax: (732) 235-5779

Nuclear Magnetic Resonance (NMR) Laboratory Site
Northeast Structural Genomics (NESG) Consortium Site

Cancer biology, influenza virus, structural biology, and structural bioinformatics

Goals of our work involve developing integrated technologies for protein structure analysis that combine bioinformatics, conformational energy calculations, nuclear magnetic resonance spectroscopy (NMR), small angle X-ray scattering (SAXS), and X-ray crystallography. The resulting structures have provided important insights into the functions of many novel gene products identified by genomic and/or bioinformatic analysis, as part of our efforts in structural genomics. We also explore applications of biophysical methods, particularly NMR spectroscopy, for characterizing conformational dynamics that underlie allosteric processes in proteins and protein-protein complexes. The resulting knowledge of structure and dynamics provides the basis for collaborations with academic laboratories and pharmaceutical companies, including collaborations in molecular virology, membrane protein structure and function, de novo protein design, and efforts to develop drugs useful in treating human diseases. Current focus areas include studies of protein complexes involved in influenza virus infection and innate immune response, protein complexes mediating viral-host chromatin interactions, networks of interacting proteins associated with cancer biology, and protein complexes formed between human synaptic proteins.

Figure 1. Alkyltransferase-like proteins (ATLs) are a novel class of DNA repair proteins related to O(6)-alkylguanine-DNA alkyltransferases (AGTs) that tightly bind alkylated DNA and shunt the damaged DNA into the nucleotide excision repair pathway. Our solution NMR structure of a bacterial ATL (cyan) provides further evidence for the conserved role of ATLs in this primordial mechanism.

Selected Publications

Marcos E, Basanta B, Chidyausiku TM, Tang Y, Oberdorfer G, Liu G, Swapna GV, Guan R, Silva DA, Dou J, Pereira JH, Xiao R, Sankaran B, Zwart PH, Montelione GT, Baker D. (2017) Principles for designing proteins with cavities formed by curved β sheets. Science 355:201-6

Ma LC, Guan R, Hamilton K, Aramini JM, Mao L, Wang S, Krug RM, Montelione GT. (2016) A second RNA-binding site in the NS1 protein of influenza B virus. Structure 24:1562-72

Cai K, Liu G, Frederick RO, Xiao R, Montelione GT, Markley JL. (2016) Structural/functional properties of human NFU1, an intermediate [4Fe-4S] carrier in human mitochondrial iron-sulfur cluster biogenesis. Structure 24:2080-91

Boel G, Letso R, Neely H, Price WN, Wong KH, Su M, Luff JD, Valecha M, Everett JK, Acton TB, Xiao R, Montelione GT, Aalberts DP, Hunt JF. (2016) Codon influence on protein expression in E. coli correlates with mRNA levels. Nature 529:358-63

Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT. (2015) Protein structure determination by combining sparse NMR data with evolutionary couplings. Nat Methods 529:358-63

Lin YR, Koga N, Tatsumi-Koga R, Liu G, Clouser AF, Montelione GT, Baker D. (2015) Control over overall shape and size in de novo designed proteins. Proc Natl Acad Sci USA 112:E5478-85

Aramini JM, Vorobiev SM, Tuberty LM, Janjua H, Campbell ET, Seetharaman J, Su M, Huang YJ, Acton TB, Xiao R, Tong L, Montelione GT. (2015) The RAS-binding domain of human BRAF protein serine/threonine kinase exhibits allosteric conformational changes upon binding HRAS. Structure 23:1382-93

Mao B, Tejero R, Baker D, Montelione GT. (2014) Protein NMR structures refined with Rosetta have higher accuracy relative to corresponding X-ray crystal structures. J Am Chem Soc 136:1893-1906

Aramini JM, Hamilton K, Ma LC, Swapna GV, Leonard PG, Ladbury JE, Krug RM, Montelione GT. (2014) F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus. Structure 22:515-25

Rosato A, Tejero R, Montelione GT. (2013) Quality assessment of protein NMR structures. Curr Opin Struct Biol 23:715-24

Montelione GT, Nilges M, Bax A, Guntert P, Herrmann T, Richardson JS, Schwieters CD, Vranken WF, Vuister GW, Wishart DS, Berman HM, Kleywegt GJ, Markley JL. (2013) Recommendations of the wwPDB NMR Validation Task Force. Structure 21:1563-70

Koga N, Tatsumi-Koga R, Liu G, Xiao R, Acton TB, Montelione GT, Baker D. (2012) Principles for designing ideal protein structures. Nature 491:222-7