Kottayil I. Varughese
Professor
Ph.D., University of Madras, India
Office: (501) 686-7160
Lab: (501) 686-7159
Email: KIVarughese@uams.edu

We are involved in the analysis of structure and function of biological macromolecules using the tools of crystallography. Our focus is on two main areas (i) Bacterial signaling (ii) Platelet interactions relevant to blood coagulation.

(i) Bacteria possess the capability to adapt to fluctuating environments that may turn hostile unexpectedly.  They do so by monitoring the environmental signals and expressing pathways needed for maximal growth under the new conditions.  One of the major regulatory mechanisms for signal recognition and response is the two-component system. In these systems, the transmission of signals is accomplished through the exchange of phosphoryl groups from one protein to another. We are studying the mode of recognition and communication between components in these signaling pathways.

(ii) Certain mutations in the A1 domain of von Willebrand Factor produce bleeding disorders. We are investigating the structural consequences of these mutations by crystallography. Additionally we are studying the interactions of the platelet glycoprotein Iba with other molecules relevant to blood clotting.

 Representative Publications

Varughese K. I., Tsigelny, I, Zhao, H. The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state. J Bacteriol. 2006 188:4970-7.

Howell, A., Dubrac, S., Noone, D., Varughese, K.I. and Devine, K.  Interactions between the YycFG and PhoPR two-component system in Bacillus subtilis: the PhoR kinase phosphorylates the non-cognate YycF response regulator upon phosphate limitations.  Mol. Microbiol.  2006.  59:1199-215. 

Celikel, R., McClintock, R. A., Roberts, J. R, Mendolicchio, G. L., Ware, J., Varughese, K. I., and Ruggeri. Z. M.,  Modulation of α-thrombin function by distinct interactions with platelet glycoprotein Ibα. Science 2003 301: 218-221.

 Varughese KI.  Molecular recognition of bacterial phosphorelay proteins.  Curr Opin Microbiol. 2002 5: 142-8.

 Celikel, R., Ruggeri, Z.M., and Varughese, K.I.  Modulation of von Willebrand factor conformation and adhesive function by an internalized water molecule.  Nature Structural Biology 2000 7: 881-884.

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