Arun Prasad Pandurangan - Investigator Scientist
MRC Laboratory of Molecular Biology
Francis Crick Avenue
Cambridge Biomedical Campus
Cambridge CB2 0QH, United Kingdom

Phone: +44 (0)122 2267822

Email: apandura@mrc-lmb.cam.ac.uk

Background


Research Areas

My research interest includes: development of computational tools to predict protein structures and ligand-receptor complexes; elucidate biological function by fitting, refining and validating atomic models into cryo-EM density maps; predict the effects of mutations on protein stability and interaction; analysis of infectious and drug resistant mutations; genome annotations.

Publications

  • Pandurangan AP*, Ochoa-Montano B, Ascher DB, Blundell TL*. (2017). SDM: a server for predicting effects of mutations on protein stability. Nucleic Acids Res Link
  • Pandurangan AP, Ascher DB, Thomas SE, Blundell TL. (2017). Genomes, Structural Biology, and Drug Discovery: Combating the Impacts of Mutations in Genetic Disease and Antibiotic Resistance. Biochem Soc Trans 45:303-311. Link
  • Jubb HC*, Pandurangan AP*, Turner MA*, Ochoa-Montano B*, Blundell TL, Ascher DB. (2016). Mutations at protein-protein interfaces: Small changes over big surfaces have large impacts on human health. Prog Biophys Mol Biol (in press) Link
  • Zeev-Ben-Mordehai T, Vasishtan D, Hernandez A, Vollmer B, White P, Pandurangan AP, Siebert A, Topf M, Grunewald K. (2016). Two distinct trimeric conformations of natively membrane-anchored full-length Herpes simplex virus 1 glycoprotein B. Proc Natl Acad Sci USA 113:4176-4181. Link
  • Pandurangan AP, Vasishtan D, Alber F, Topf M. (2015). ϒ-TEMPy: simultaneous fitting of components in 3D-EM maps of their assembly using a genetic algorithm. Structure 23:2365-2376. Link
  • Farabella I, Vasishtan D, Joseph AP, Pandurangan AP, Sahota H, Topf M. (2015). TEMPy: a Python Library for Assessment of 3D Electron Microscopy Density Fits. J Appl Cryst 48:1314-1323. Link
  • Leung C, Dudkina NV, Lukoyanova N, Hodel AW, Farabella I, Pandurangan AP, Dino Osmanovic D, Reboul C, Dunstone MA, Topf M, Lonnen R, Andrew PW, Saibil H, and Hoogenboom BW. (2014). Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin. eLife 2014;10.7554/eLife.04247. Link
  • Mortensen M, Iqbal F, Pandurangan AP, Hannan S, Huckvale R, Topf M, Baker JR, Smart T. (2014). Photo-antagonism of the GABAA receptor. Nature Commun 5:4454. Link
  • Pandurangan AP*, Shakeel S*, Butcher SJ and Topf M. (2014). Combined approaches to flexible fitting and assessment in virus capsids undergoing conformational change. J Struct Biol 185:427-439. (*Equal contribution). Link
  • Thalassinos K, Pandurangan AP, Xu M, Alber F, Topf M. (2013). Conformational States of macromolecular assemblies explored by integrative structure calculation. Structure 21:1500-1508. Link
  • Maurer UE, Zeev-Ben-Mordehai T, Pandurangan AP, Cairns TM, Hannah BP, Whitbeck JC, Eisenberg RJ, Cohen GH, Topf M, Huiskonen JT and Grunewald K. (2013). The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction. Structure 21:1396-1405. Link
  • Pandurangan AP* and Topf M*. (2012). RIBFIND: a web server for identifying rigid bodies in protein structures and to aid flexible fitting into cryo EM maps. Bioinformatics 28:2391-2393. (*Corresponding authors). Link
  • Pandurangan AP and Topf M. (2012). Finding rigid bodies in protein structures: Application to flexible fitting into cryoEM maps. J Struct Biol 177:520-531. Link
  • Seitsonen J, Shakeel S, Susi P, Pandurangan AP, Sinkovits R, Hyvonen H, Laurinmaki P, Yla-Pelto J, Topf M, Hyypia T and Butcher S. (2012). Structural analysis of coxsackievirus A7 reveals changes associated with uncoating. J Virol 86:7207-7215. Link
  • Ramya L, Nehru VS, Arun Prasad P , Kanagasabai V and Gautham N. (2010). MOLS sampling and its applications in structural biophysics. Biophys Rev 2:169-179. Link
  • Nehru VS, Arun Prasad P and Gautham N. (2009). Protein-ligand docking using mutually orthogonal Latin squares (MOLSDOCK). J Chem Inf Model 49:2687-2694. Link
  • Arun Prasad P and Gautham, N. (2008). A new peptide docking strategy using a mean field technique with mutually orthogonal Latin square sampling. J Comput-Aided Mol Des 22:815-829. Link
  • Arun Prasad P, Kanagasabai V, Arunachalam J and Gautham N. (2007). Exploring the conformational space using a mean field technique with MOLS sampling. J Biosci 32:909-920. Link
  • Kanagasabi V, Arunachalam J, Prasad PA and Gautham N. (2007). Exploring the conformation of protein loops using a mean field with MOLS sampling. Proteins 67:908-921. Link
  • The NMITLI-Biosuite Team*. (2007). BioSuite: A comprehensive bioinformatics software package (A unique industry-academia collaboration). Current Science 92:29-38 [*The author list is long as the project was part of a industry-academia collaboration]. Link
  • Arun Prasad P, Vengadesan K and Gautham N. (2005). MOLS - A program to explore the potential energy surface of a peptide and locate its low energy conformations. In Silico Biology 5:401-405. Link


Organisations and funding