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Department of Biochemistry and Molecular Biophysics

Department of Biochemistry & Molecular Biophysics
141 Chalmers Hall
1711 Claflin Rd.
Manhattan, KS 66506
785-532-6121
785-532-7278 fax
biochem@k-state.edu

Biotechnology Core Facility
206 Burt Hall
785-532-5956
785-532-6297 fax

Biomolecular NMR Facility
37 Chalmers Hall
785-532-2345

Saurav Misra, Ph.D., Adjunct Associate Professor

Saurav Misra, Ph.D.

Contact information

Email: misras@ksu.edu

Education

B.S. (Physics) 1991, Ohio University, Athens, OH
B.S. (Electrical Engineering) 1991, Ohio University, Athens, OH
Ph.D. (Biophysics) 1997, University of Illinois at Urbana-Champaign, Urbana, IL

Areas of specialty

  • Protein quality control and protein degradation
  • Intracellular protein trafficking and targeting
  • Structural basis of protein-protein and protein-drug interactions
  • Macromolecular structure determination

We investigate a broad theme in cell biology: How cells regulate the quality and disposal of their constituent proteins. We are particularly interested in the quality control of proteins that are intrinsically prone to aggregation or misfolding, a molecular basis of pathology in many diseases including neurodegenerative disorders, cardiomyopathies and cystic fibrosis. We are also interested in how protein quality control processes oppose cellular transformation, oncogenesis and cancer by regulating the cellular levels of both pro- and anti-oncogenic signaling proteins. Much of our research focuses on determining how intracellular chaperones, which survey protein quality, cooperate with the ubiquitin-proteasome machinery to “decide” whether and how proteins are folded, preserved or degraded. A major current focus is CHIP (also called STUB1), a ubiquitinating protein that targets misfolded proteins bound to intracellular chaperones. We investigate how CHIP interacts with chaperones, with its protein targets, and with regulatory “cochaperones” that modulate CHIP’s activity. Our eventual goal is to identify small-molecule or peptide-based therapeutics that will enable us to selectively control CHIP’s activity in specific pathological and disease contexts.

A second research interest in the group is to investigate how chaperones and ubiquitinating proteins function in innate immune signaling pathways. While we study how such proteins interact with other components of innate immune pathways, we are particularly interested in how pathogenic organisms may evade innate immunity by subverting host cell chaperones and ubiquitinating proteins. Our current interest is to elucidate the mechanisms utilized by the nonstructural proteins (NS1 and NS2) of respiratory syncytial virus (RSV), which interact directly with several host ubiquitinating proteins to attenuate antiviral innate immune responses in infected cells. RSV is an important cause of respiratory ailments in infants, young children, the elderly and immuno-compromised individuals. Our goal is to discover new anti-RSV compounds. We also seek to better understand how to generate attenuated RSV strains that can be utilized for the development of vaccines against RSV.

Students working in the lab will learn techniques in basic biochemistry and protein chemistry, structural biology, and biophysical methods to investigate protein structure, function, and protein-protein interactions.

Selected publications

H. Zhang, J. Amick, R. Chakravarti, S. Santarriaga, S. Schlanger, C. McGlone, M. Dare, J.C. Nix, K.M. Scaglione, D.J. Stuehr, S. Misra* , R.C. Page* (2015) A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. Structure 23, 472-82. (*co-corresponding)

A. Sarkar, Y. Dai, M.M. Haque, F. Seeger, A. Ghosh, E.D. Garcin, W.R. Montfort, S.L. Hazen, S. Misra, D.J. Stuehr. (2015) Heat Shock Protein 90 associates with the Per-Arnt-Sim domain of heme-free soluble Guanylate Cyclase: Implications for enzyme maturation. J. Biol. Chem. 290, 21615-28.

C. Zheng, R.C. Page, V. Das, J.C. Nix, E. Wigren, S. Misra, B. Zhang. (2013) Structural characterization of carbohydrate binding by LMAN1 protein provides new insights into the endoplasmic reticulum export of Factors V (FV) and VIII (FVIII). J. Biol. Chem. 288, 20499-509.

P.A. Klenotic, R.C. Page, W. Li, J. Amick, S. Misra*, R.L. Silverstein* (2013) Molecular basis of antiangiogenic thrombospondin-1 type 1 repeat domain interactions with CD36**. Arterioscler. Thromb. Vasc. Biol. 33, 1655-62. (*co-corresponding); (**cover-article)

R.C. Page, J.N. Pruneda, J. Amick, R.E. Klevit, S. Misra. (2012) Structural insights into the conformation and oligomerization of E2~ubiquitin conjugates. Biochemistry 51, 4175-87.

C. Liu, S. Swaidani, W. Qian, Z. Kang, P. Sun, Y. Han, C. Wang, M.F. Gulen, W. Yin, C. Zhang, P.L. Fox, M. Aronica, T.A. Hamilton, S. Misra, J. Deng, X. Li (2011) A CC’ loop decoy peptide blocks the interaction between Act1 and IL17RA to attenuate IL-17- and IL-25 induced inflammation. Science Signal. 4:ra72.

L. Smith, R.C. Page, Z. Xu, E. Kohli, P. Litman, J.C. Nix, S.S. Ithychanda, J. Liu, J. Qin, S. Misra*, C.M. Liedtke*. (2010) Biochemical basis of the interaction between cystic fibrosis transmembrane conductance regulator and immunoglobulin-like repeats of filamin. J. Biol. Chem. 285, 17166-76. (*co-corresponding)

Z. Xu, R.C. Page, M.M. Gomes, E. Kohli, J.C. Nix, A.B. Herr, C. Patterson, S. Misra. (2008) Structural basis of nucleotide exchange and client binding by the novel Hsp70-cochaperone Bag2. Nature Struct. Molec. Biol. 15:1309-17.

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