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A Mi2b loop-3 mutant

[ PDB file ] [ PubMed link ]

Shown is the structure of a mutant of Mi2-P2, with the second flexible loop (called L3) replaced by the corresponding region from another PHD domain from the protein WSTF. This structure shows that the PHD fold is indeed preserved in the mutant. The backbone of L3-WSTF overlays well with Mi2b-P2 except for some minor differences observed at residues 20-22 and 43-46, which correspond to the two flexible regions (shown in orange and purple).

The third zinc finger of BKLF

[ PDB file ] [ PubMed link ]

BKLF is a transcriptional repressor involved in erythropoiesis. It has been shown to interact with both DNA (CACCC boxes) and the C-terminal zinc finger of GATA-1. We have determined its solution structure as a first step towards characterizing this interaction. In addition, we have shown that variants of this domain in which the final zinc-ligating histidine is mutated to residues such as asparagine and alanine are still functional in binding both GATA-1 and, in the context of a 3-zinc-finger construct, DNA.

The LMO4:ldb1 complex

[ PDB file ] [ PubMed link ]

The transcriptional regulator LMO4 consists entirely of two LIM domains, and must bind to the partner protein ldb1 in order to be transported into the nucleus and carry out its role in the regulation of lymphogenesis. We have determined the structure of a complex formed betwen full-length LMO4 and the LMO4-binding region of ldb1 using X-ray crystallography. The interaction interface is completely extended, and the ldb1 peptide (yellow) forms additional beta-strands on beta-hairpins present in both of the LMO4 LIM domains. This tandem beta-zipper arrangement has been observed in one other recent structure - a bacterial pathogen that binds cellular fibronectin repeats (Potts et al., Nature 2003, 423, 177). This structure can now serve as a scaffold from which inhibitors of the LMO4:ldb1 interaction may be designed.

The FOG-TACC3 complex

[ PDB file ] [ PubMed link ]

FOG-1 is vital for the development of red blood cells and platelets. Originally identified as a Friend of GATA, GATA-independent functions are now emerging. Recently, we identified TACC3 as a protein partner of FOG-1. FOG-1 uses its third (of nine) ZnF to bind the coiled-coil domain of TACC3. The structure of FOG-1 finger 3 (left) shows that it is a typical classical CCHH finger (BMRB 6216). NMR and mutagenesis data identified the residues important for the interaction between FOG-1 (yellow) and TACC3 (blue) and this allowed us to use HADDOCK to calculate the structure of the FOG-TACC3 complex (right).

AHSP - alpha-hemoglobin stabilizing protein

[ PDB file ] [ PubMed link ]

Red blood cells contain an excess of the alpha-chain of hemoglobin over the beta-chain. It is known that excess alpha-globin is unstable, and its precipitation can lead to membrane damage and apoptosis. This phenomenon is the root of the beta-thalassemia phenotype, in which sufferers cannot make sufficient beta-globin. How is the normal excess of alpha-globin kept 'safe'? The answer seems to lie in AHSP - a protein that appears to act as a specific chaperone of alpha-globin, binding to the globin and preventing its precipitation. We have determined the structure of AHSP and used NMR titration methods and mutagenesis to reveal which residues are involved in mediating this specific interaction. In addition, as part of a collaboration with Yigong Shi at Princeton, the structure of the AHSP:a-globin complex was determined by X-ray crystallography. This structure confirmed many of our predictions based on biophysical analysis of the interaction. Collaborative work is also ongoing with Peter Lay in the School of Chemistry at USyd to examine the properties of the metal-binding site in the complex.

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 - 65] [66 - 69]

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Lastest update: "Lab members page", on 24th Aug 2020.

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© W. Yung 2002