Administration and Staff

Klara Briknarova

Klara Briknarova

Associate Professor

Phone: (406) 243-4408
Office: CHEM 111

Current Position

Associate Professor, Department of Chemistry and Biochemistry


Proteins and Enzymes (BCH 582)

Physical Biochemistry (BCH 581)

Personal Summary

Klára Briknarová came to the University of Montana in November 2005. Klára received her undergraduate education from School of Mathematics and Physics at Charles University in Prague, Czech Republic. She carried out graduate studies in the laboratory of Professor Miguel Llinás at Carnegie Mellon University, and earned her PhD. in Biophysics/Chemistry in 1999. She then worked as a postdoctoral fellow in the laboratory of Professor Kathryn R. Ely at the Burnham Institute. Klára is a biochemist and structural biologist.


M.S. in Biophysics and Chemical Physics, School of Mathematics and Physics, Charles University, Prague, Czech Republic, 1992

Ph.D. in Chemistry/Biophysics, Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA, 1999

Postdoctoral training, The Burnham Institute (now Sanford Burnham Prebys Medical Discovery Institute), La Jolla, CA, 1999-2005

Research Interests

  • Protein structure and function
  • Structural biology


Molecular mechanism of transcriptional regulation by EHMT and PRDM proteins

A question of particular interest is how cell identity is established and maintained at the molecular level. Brain, heart or fat cells are remarkably different yet they all start with the same genes. How do different cells and tissues remember what they are, and what keeps them from going astray? Gaining insight into how cell-type specific transcription programs are determined remains a major challenge for life sciences today. Transcriptional regulation and in particular epigenetics (heritable changes in gene expression that occur without changes in DNA sequence) have become an area of very intensive research that has large implications for stem cell biology, development, and various human diseases including cancer. One large group of transcriptional regulators that are involved in establishment of cell-type specific transcription programs are proteins with a SET domain or the closely related PR domain. We investigate the structure and function of several of these proteins using biochemical methods, NMR spectroscopy and X-ray crystallography.

A cartoon model of the PR domain from PRDM3

Protein interactions and conformational changes in fibronectin fibril formation

Fibronectin is a large multidomain extracellular matrix glycoprotein that is essential for vertebrate development. It also serves an important function in tissue repair and plays a role in other physiological and pathological processes including cancer. Fibronectin is secreted as a soluble dimer and is assembled into fibrils on the surface of cells in a process that requires cell-generated tension. Despite the essential function of fibronectin and its applications in biomaterial engineering and medicine, the molecular basis of its conversion to fibrils is poorly understood, and the exact arrangement of fibronectin molecules within fibrils is not known. We study the structure of fibronectin in solution and its organization in fibrils using a range of techniques including fluorescence microscopy, crosslinking, NMR spectroscopy, X-ray crystallography, and cryo-electron microscopy.

Fibronectin fibrils assembled by fibroblasts and imaged by fluorescence microscopy

Selected Publications

Kerchner, K.M., Mou, T.C., Sun, Y., Rusnac, D.V., Sprang, S.R. and Briknarová, K. (2021) The structure of the cysteine-rich region from human histone-lysine N-methyltransferase EHMT2 (G9a). J. Struct. Biol X 5, 100050.

Danielson, T.A., Stine, J.M., Dar, T.A., Briknarova, K. and Bowler, B.E. (2017) Effect of an imposed contact on secondary structure in the denatured state of yeast iso-1-cytochrome c. Biochemistry 56, 6662-6676.

Stine, J.M., Ahl, G.J.H., Schlenker, C., Rusnac, D.V. and Briknarová, K. (2017) The interaction between the third type III domain from fibronectin and anastellin involves b-strand eexchange. Biochemistry 56, 4667-4675.

Stine, J.M., Sun, Y., Armstrong, G., Bowler, B.E. and Briknarová, K. (2015) Structure and unfolding of the third type III domain from human fibronectin. Biochemistry 54, 6724-6733.

Sun, Y., Stine, J.M., Atwater, D.Z., Sharmin, A., Ross, J.B.A. and Briknarová, K. (2015) Structural and functional characterization of the acidic region from the RIZ tumor suppressor. Biochemistry 54, 1390-1400.

Thomas, C.J., Briknarová, K., Hilmer, J.K., Movahed, N., Bothner, B., Sumida, J.P., Tall, G.G. and Sprang, S.R. (2011) The nucleotide exchange factor Ric-8A is a chaperone for the conformationally dynamic nucleotide-free state of Gai1. PLoS ONE 6, e23197.

Briknarová, K., Atwater, D.Z., Glicken, J.M., Maynard, S.J. and Ness, T.E. (2011) The PR/SET domain in PRDM4 is preceded by a zinc knuckle. Proteins 79, 2341-2345.

Briknarová, K., Thomas, C.J., York, J. and Nunberg, J.H. (2011) Structure of a zinc-binding domain in the Juní­n virus envelope glycoprotein. J. Biol. Chem. 286, 1528-1536.

Briknarová, K., Zhou, X., Satterthwait, A., Hoyt, D.W., Ely, K.R. and Huang, S. (2008) Structural studies of the SET domain from RIZ1 tumor suppressor. Biochem. Biophys. Res. Commun. 366, 807-813.

Briknarová, K., Nasertorabi, F., Havert, M.L., Eggleston, E., Hoyt, D.W., Li, C., Olson, A.J., Vuori, K. and Ely, K.R. (2005) The serine-rich domain from Crk-associated substrate (p130Cas) is a four-helix bundle. J. Biol. Chem. 280, 21908-21914

Derunes, C., Briknarová, K., Geng, L., Li, S., Gessner, C.R., Hewitt, K., Wu, S., Huang, S., Woods, V.I. Jr. and Ely, K.R. (2005) Characterization of the PR domain of RIZ1 histone methyltransferase. Biochem. Biophys. Res. Commun. 333, 925-934.

Briknarová, K., Åkerman, M.E., Hoyt, D.W., Ruoslahti, E. and Ely, K.R. (2003) Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors. J. Mol. Biol. 332, 205-215.

Briknarová, K., Takayama, S., Homma, S., Baker, K., Cabezas, E., Hoyt, D.W., Li, Z., Satterthwait, A.C. and Ely, K.R. (2002) BAG4/SODD protein contains a short BAG domain. J. Biol. Chem. 277, 31172-31178.

Briknarová, K., Takayama, S., Brive, L., Havert, M.L., Knee, D.A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D.W., Satterthwait, A.C., Llinás, M., Reed, J.C. and Ely, K.R. (2001) Structural analysis of BAG1 co-chaperone and its interactions with Hsc70 heat shock protein. Nature Struct. Biol. 8, 349-352.