I am Safal Shrestha

Graduate Student,Bioinformatician,Aspiring Structural Biologist,Real Madrid Fan,A Fellow Craniac

Name: Safal Shrestha

Profile: Graduate Research Assistant, Institute of Bioinformatics, University of Georgia

Email: safal.shrestha@uga.edu

Skills

About me

I am a graduate student pursuing a PhD in Dr. Natarajan Kannan's lab at the University of Georgia. I am studying the evolution of regulation and substrate specificity in an ancient family of kinase fold enzymes called Fructosamine-3-kinases (FN3Ks).

When I am not in lab, I play 7V7 competitive soccer with fellow graduate students for Inter United @YWCO. I am that striker who has more assists than goals😀. Frasier is my all time favourite show, and Niles is my favourite character.

Preprints and Publications

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A novel redox-active switch in Fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily

In this study, we solved the crystal structure of FN3K homolog from Arabidopsis thaliana and showed that the enzyme is a novel strand exchange dimer mediated through disulfide bridges. We showed biochemically that the enzyme is redox regulated. Based on sequence conservation, we identified equivalent cysteine in human ortholog and showed that enzyme is also redox regulated.

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Cataloguing the dead: breathing new life into pseudokinase research

In this review/study, we applied Bayesian statistics and identified family specific patterns for pseudokinases EphA10, EphB6, Tribbles, and PSKH2.




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Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity

In this study, in collaboration with Dr. Eyers at the University of Liverpool, we looked at the conservation and the extent of distribution of redox-active cysteine residues in the activation loop of protein kinases.

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Nucleotide binding, evolutionary insights and interaction partners of the pseudokinase Unc-51-like kinase 4

In collaboration with Dr. Stefan Knapp, we characterized the evolutionary history of the pseudokinase ULK4 and identified the co-evolution of activation loop insertion with concomitant loss of key catalytic residues.