Structural Biology

dsRNA binding proteins


BIO here

-DPhil at Oxford University (1999-2003), Supervised by Prof. Louise Johnson

-Post-doctoral work with Elena Conti initially at EMBL Heidelberg (2004-2007) and later at the MPI for biochemistry in Martinsried (2007-2010)

-MRC career development Fellow at Wellcome Trust centre for Cell Biology in Edinburgh (2011-2016)

-WT Senior Research Fellow at Wellcome Trust centre for Cell Biology in Edinburgh (2016-present)


Structural biology, protein expression and purification, in vitro charactersation of protein-nucleic acid interactions


Kruusvee V§, Lyst MJ§, Taylor C, Tarnauskaite Ž, Bird AP* and Cook AG* (2017) Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett syndrome and related disorders. PNAS 114:E3243-E3250. doi: 10.1073/pnas.1700731114 PMC5402415 *Joint corresponding, § joint first author

McCaughan UM, Jayachandran U, Shchepachev V, Chen Z.A, Rappsilber J, Tollervey D and Cook AG (2016) Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases. Nat Commun. 7:11789. doi: 10.1038/ncomms11789. PMC4895721

Jayachandran U, Grey H and Cook AG (2015) Nuclear Factor 90 uses an ADAR2-like binding mode to recognize specific bases in dsRNA. Nucl. Acids Res. doi: 10.1093/nar/gkv1508 PMC4770229

Hector RD, Burlacu E, Aitken S, Le Bihan T, Tuijtel M, Zaplatina A, Cook AG and Granneman S (2014) Snapshots of pre-rRNA structural flexibility reveal eukaryotic 40S assembly dynamics at nucleotide resolution. Nucl. Acids Res. doi: 10.1093/nar/gku815 PMC4231735

Wolkowicz UM and Cook AG (2012) NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold. Nucl. Acids Res. 40:9356-68 PMC3467086

Cook AG, Fukuhara N, Jinek M and Conti E (2009). Structures of the tRNA export factor in the nuclear and cytosolic states. Nature 461, 60-65

Cook A§, Fernandez E§, Lindner D, Ebert J, Schlenstedt G & Conti E (2005) The structure of the nuclear export receptor Cse1 in its cytoplasmic state reveals a closed conformation incompatible with cargo binding. Mol. Cell. 18:355-67 § joint first author