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Recent news

25 July, 2014: Jacqui invited to speak at the triennial GATA meeting in 2015

1 May, 2014: Marylène's paper on designer RNA-binding proteins has been accepted in Angew. Chem.

1 May, 2014: Soumya is given the nod



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Show structures: [1 - 5] [6 - 10] [11 - 15] [16 - 20] [21 - 25] [26 - 30] [31 - 35] [36 - 40] [41 - 45] [46 - 50] [51 - 55] [56 - 60] [61 - 62]
Stripped down CHANCE domain #2

[ PDB file ] [ PubMed link ]

This is a second minimalised version of the CHANCE domain. This time, 13 of the 25 residues have been mutated (mostly to alanine), and the fold is retained. These two stripped down domains retain only the zinc-binding residues and the residues that make significant numbers of contacts.

Designed-for-function CHANCE 2 (DFF2)

[ PDB file ] [ PubMed link ]

This is one of the first CHANCE peptides that was designed to emulate the binding function of another protein. The N-terminal nucleocapsid domain (NUC1, left) of the HIV-1 nucleocapsid protein is able to bind to a short oligonucleotide from the virus' genome. We identified the binding residues from NUC1 and 'grafted' them onto our CHANCE domain, in an arrangement that appeared to mimic their spatial orientation in the NUC1 protein. The structure of DFF2 shows that the grafted residues do indeed form a surface that bears a reasonable resemblance to the template protein. Unfortunately, NMR titration data indicated that DFF2 was not actually able to specifically recognize the NUC1 target oligonucleotide. Back to the drawing board!

Designed-for-function CHANCE 5 (DFF5)

[ PDB file ] [ PubMed link ]

This CHANCE peptide was designed to mimic the GATA-binding surface of the transcriptional repressor U-shaped. We have previously defined the surface involved in this interaction, and we attempted to transplant this surface onto the minimal CHANCE domain. NMR structural work showed both that DFF5 was well-folded and that the grafted residues occupied positions that were similar (although not identical) to those found in the native USF1 protein. In the picture, the grafted residues are shown overlayed with the same residues from USF1.

Designed-for-function CHANCE 7 (DFF7)

[ PDB file ] [ PubMed link ]

This CHANCE peptide was one of two (+DFF5) designed to mimic the GATA-binding surface of the transcriptional repressor U-shaped. NMR structural work showed both that DFF7 was well-folded (right) and that the grafted residues occupied positions that were similar (although not identical) to those found in the native USF1 protein (left). Both DFF5 and DFF7 displayed measureable binding to GATA-1, as judged by NMR titration experiments, although the nature of the binding may not be as specific as intended.

EAS: a fungal hydrophobin

[ PDB file ] [ PubMed link ]

Hydrophobins are small fungal proteins that form polymeric fibrils, known as rodlets. These rodlets form a matted coating on the surface of aerial structures like air-dispersed spores. The coating is extremely amphipathic, with an outward facing hydrophobic surface that "water-proofs" the spores. The coating is also extremely robust and is being considered for material science applications. Our structure of the monomeric hydrophobin from Neurospora crassa shows that it is made up entirely of beta structure (top right), forming a 4-stranded beta-barrel. The structure contains two very flexible loops (seen top left), which may play a role in fibril formation. The electrostatic surface properties of the EAS structure are also consistent with the amphipathic nature of the rodlets (bottom), and have allowed us to create a model for fibril formation (see below).

Show structures: [1 - 5] [6 - 10] [11 - 15] [16 - 20] [21 - 25] [26 - 30] [31 - 35] [36 - 40] [41 - 45] [46 - 50] [51 - 55] [56 - 60] [61 - 62]

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Lastest update: "News", on 28th Jul 2014.


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