Fionna has just had her first paper published from her postdoc with Fred Allain at the ETH in Zurich – in NSMB, no less! While simultaneously juggling a small child (not literally) she has published her structure of the zinc knuckle domains of Lin28 (an inhibitor of miRNA biosytnthesis) bound to a pre-miRNA from Let7 […]
Lorna’s paper describing the multi-protein complexes formed by LMO2, GATA-1, LDB1 and – thrown in for good measure – FOG1 has appeared in the latest issue of PNAS – check it out here. You can also have a look at the structure in our structure gallery – number 43.
…then look no further than the latest blockbuster from Mackay and Segal. Packed with juicy material on the bipartite selection of zinc fingers by phage display, the lowdown on inhibition of viral transcription by zinc finger proteins and the shocking tale of transgenic mice expressing an artificial zinc finger protein that targets an endogenous gene, […]
The journal RNA selected Fionna’s crystal structure of a ZRANB2 zinc finger bound to RNA as the cover illustration for their March 2010 issue. Today the cover of RNA, tomorrow the centrefold of Cleo…
After a long reviewing process, Dr Liza Cubeddu, a National Breast Cancer Foundation Fellow in Jacqui’s lab, has just seen some of her work finally appear in Nature (PubMed). This paper describes a new human single-stranded DNA binding protein that is essential for genomic stability – the work originated from Liza’s previous life in St […]
One of our most prized structures, the GATA:FOG zinc finger complex, features in the Protein Data Bank’s Molecule of the Month section for March 2007. Check it out! A couple of our recent reviews of the field (Sunde and Matthews and Gamsjaeger et al.) were also used to create the feature.
After about 7 years of painstaking work (!), we have finally been able to solve and publish the structure of the complex formed between the N-terminal zinc finger of GATA-1 and a classical finger from FOG. This work was made very difficult by the weak nature of the complex (~104-105 M-1), which presented line-broadening problems. […]
The structure of the complex formed between full-length LMO4 and the LMO4-binding region of ldb1 was published recently in EMBO J. This structure revealed a very unusual binding mode – a tandem beta-zipper, in which the ldb1 forms additional beta-strands to add on to hairpins in both of the LIM domains. The structure provides an […]
Our most recent paper, a collaboration with Peter Karuso, on the solution properties of DNA-binding ruthenium complexes, made the cover of Dalton Transactions, a Royal Society of Chemistry journal.