Renos Savva

Senior Lecturer

Based at Birkbeck

Personal Website

Structure and sequence in biological macromolecular interaction

Renos Savva is principal investigator with a focus upon structural biology centred upon x-ray crystallography, combined with bioinformatics and synthetic protein manipulation and design.

Biological macromolecules interact precisely at the atomic level based upon structural and biophysical properties, which can be interrogated in silico by signatures such as sequence motif conservation at the amino acid and nucleotide level. Significant changes in recognised motif signatures can either support essentially identical structural configurations from a chemical perspective, or else may be indicative of novel functional characteristics. Furthermore, synthetic library methods may also shed light upon essential properties of sequence to structure relationships. We apply structural biology, bioinformatics and synthetic methods to generate deeper insight into biophysical and evolutionary hidden signatures essential to macromolecular interactions.

Systems currently under study include uracil-DNA repair and its relationship to essential biological processes such as replication, especially in viruses. We also study the phenomenon of viral antagonism of cellular uracil-DNA repair and its evolutionary context. We apply synthetic library methods to decipher the nature of motif conservation and evolution, as well as to repurpose large-scale macromolecular assemblies.

Dr Savva is also involved in industrial outreach, for the purposes of scientific collaboration as well as being programme coordinator for the MSc Bio-business at Birkbeck, and sitting on the BBSRC LIDo Phd programme's industry, impacts and internships committee. Dr Savva is also active in local PhD and postdoctoral researcher career development.

Selected publications

A structurally conserved motif in γ-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping
Earl, C., Bagnéris, C., Zeman, K., Cole, A., Barrett, T., Savva, R.
Nucleic Acids Research (2018) 46 (8):4286–4300
Architecturally diverse proteins converge on an analogous mechanism to inactivate Uracil- DNA glycosylase
Cole, A.R., Ofer, S., Ryzhenkova, K., Baltulionis, G., Hornyak, P., Savva, R.
Nucleic Acids Research (2013) 41 (18):8760-8775
A combinatorial method to enable detailed investigation of protein-protein interactions
Maclagan, K., Tommasi, R., Laurine, E., Prodromou, C., Driscoll, P.C., Pearl, L.H., Reich, S., Savva, R.
Future Medicinal Chemistry (2011) 3 (3):271-282