Protein structure, function and engineering lab Structure gallery
Home

Research Interests

Structure Gallery

Publications

Research Methods

Current lab members

Past lab members

Excursions/photos

Contact/find us

News

Internal

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



Random photo

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]
Data-driven model of the MED-1:DNA complex

[ PDB file ] [ PubMed link ]

MED-1 is a GATA-family transcription factor that is essential for development in Caenorhabditis elegans. It's single GATA-type zinc finger was shown by Morris Maduro to bind to a long and slightly divergent DNA site (GTATACTTTT), compared to the well-known consensus for mammalian GATA-family zinc fingers (AGATAA). We used a combination of NMR spectroscopy, gel shifts and mutagenesis to demonstrate that the MED-1 zinc finger forms an additional C-terminal helix, which is induced only upon binding to DNA. This helix is inserted into the major groove of DNA to bind to the 3' end of the recognition sequence. These data demonstrate the difficulties in predicting the structures of protein complexes from sequence data alone - the additional helix was not predicted by secondary structure prediction algorithms.

A new class of ssRNA-binding domain

[ PDB file ] [ PubMed link ]

The two zinc fingers of ZRANB2 (formerly known as ZNF265) can bind to single-stranded RNA with high sequence specificity. We have determined the structure of one of these fingers bound to its RNA target site (AGGUAA - determined by SELEX). The structure reveals a new class of RNA-binding domain. This ZnF forms a unique guanine-Trp-guanine aromatic stack, and the core nucleotides (GGU) are recognized by an extensive network of protein side-chain hydrogen bonds. Also notable are the two-headed hydrogen bonds that are formed between arginine side-chains and the two guanines - these interactions appear to provide strong selection for guanine in those positions.

The FOG1-RbAp48 complex

[ PDB file ] [ PubMed link ]

FOG1 is a coregulator protein that assists the transcription factor GATA1 in the control of gene expression during erythroid development. Gerd Blobel, a collaborator of ours in Philadelphia, showed that at least part of the mechanism by which FOG1 regulates GATA1 expression is through its ability to recruit the multiprotein NuRD (Nucleosome Remodeling and Deacetylase) complex. We have determined the structure of a complex formed between the NuRD-binding region of FOG1 (residues 1-15) and the RbAp48 component of the NuRD complex. RbAp48 forms a beta-propellor and a basic sequence in the FOG1 peptide docks into a cavity at one end of the propellor.

The first PHD domain of CHD4

[ PDB file ] [ PubMed link ]

The Nucleosome Remodeling and Deacetylase (NuRD) complex is essential for the normal regulation of gene expression in a wide range of organisms (even plants!). We are slowly trying to build up a picture of how NuRD works at a mechanistic level. One of the NuRD components, CHD4, contains two PHD-type zinc-finger domains. This picture shows the structure of the first PHD domains, which we have shown in collaboration with Tanya Kutateladze from the University of Colorado at Denver can recognize the N-terminal tail of histone H3.

The mechanism of H3K9Me3 recognition by CHD4

[ PDB file ] [ PubMed link ]

The Nucleosome Remodeling and Deacetylase (NuRD) complex is essential for the normal regulation of gene expression in a wide range of organisms (even plants!). We are slowly trying to build up a picture of how NuRD works at a mechanistic level. One of the NuRD components, CHD4, contains two PHD-type zinc-finger domains. In collaboration with Tanya Kutateladze from the University of Colorado at Denver, we have shown that one of these two PHD domains can recognize the N-terminal tail of histone H3 when specifically modified by trimethylation of K9 (a repressive mark). We have determined the structure of the PHD:H3 tail complex, showing how the methylated K9 is recognized (on the right of the pic).

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]

Back to top



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


Flag Counter
0.666104s
© W. Yung 2002
School of MB
USyd