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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]
The crossed finger of ZNF265

[ PDB file ] [ PubMed link ]

ZNF265 is a mammalian splicing factor, which contains an Arg-Ser rich domain and a putative double zinc finger motif that is capable of binding to RNA (putting it in the SR class of proteins). Shown here is the structure of one of the two zinc fingers. The structure comprises two beta-hairpins, crossing each other at an angle of ~80 degrees, and sandwiching a single zinc atom. The fold is unlike any known zinc-binding motifs and we have termed it the crossed finger. Remarkably, the positions of the residues shown in space-fill mimic the RNA-binding residues of the unrelated dsRBM (double-stranded RNA-binding module) domain, indicating the convergent evolution of a binding surface on different scaffolds.

FLIN2: a transcriptional complex

[ PDB file ] [ PubMed link ]

FLIN2 (PDB: 1J2O) is an engineered intramolecular complex comprising a fusion of the LID domain of ldb1 and the N-terminal LIM domain of LMO2. The solution structure of FLIN2 shows that ldb1-LID (yellow ribbon) binds to the LMO2 LIM1 domain (surface representation) in an extended fashion. Half of the interaction interface involves predominantly backbone-backbone and side-chain hydrophobic interactions, the other involves mainly electrostatic interactions.

FLIN4: a(nother!) transcriptional complex

[ PDB file ] [ PubMed link ]

We have solved the structure of a complex of the transcription regulators LMO4 and ldb1 (PDB: 1M3V). To do this we engineered FLIN4, a fusion of the LID domain of ldb1 and the N-terminal LIM domain of LMO4. The structure of FLIN4 shows that ldb1-LID (yellow) binds to both Zn1 (cyan) and Zn2 (magenta) of LMO4-LIM1 in an extended fashion with ldb1-LID forming a short b-strand that extends a b-hairpin present in LMO4-LIM1.

YPM Superantigen

[ PDB file ] [ PubMed link ]

Bacterial superantigens are involved in overstimulating T cells. YPM has a structure that is unique amongst classical superantigens. Typical superantigens consist of 2 b-strand domains and a central α-helix. However YPM consists of 8 antiparallel β-strands that form a jelly roll motif. There are 2 main regions in the YPM structure, one that is quite rigid and another that undergoes intermediate exchange. The unique structure of YPM suggests that it may activate T cells through a mechanism that is distinct from other superantigens.

A PHD domain from Mi2

[ PDB file ] [ PubMed link ]

We have used NMR methods to determine the solution structure of the second PHD finger from the transcriptional regulator Mi2b. This structure indicates that PHD fingers contain two relatively flexible loop regions (shown in orange and red) and a conserved stable core that ligates two zinc atoms (zinc ligation residues are shown in yellow and green). By using a strategy of mutagenic substitution and expansion, we have also shown that a wide variety of mutations in these loops can be tolerated without major disruption of the PHD fold. If you want to see for yourself, the solution structure of one of these mutants is shown in the next figure!

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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