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Crystal Structure of Human Methaemoglobin Complexed with the Second NEAT Domain of IsdH from Staphylococcus aureus

[ PDB file ] [ PubMed link ]

This structure shows that the second NEAT domain of IsdH is involved in recognizing hemoglobin rather than extracting heme/iron. That task falls to the third NEAT domains (as elegantly shown from Claire Dickson's structure in the same paper).

Human Alpha-Haemoglobin Complexed with the First NEAT Domain of IsdH from Staphylococcus aureus

[ PDB file ] [ PubMed link ]

Another step in the story of understanding how Staph aureus steals iron from host red blood cells.

X-ray crystal structure of an Isl1-Ldb1 complex

[ PDB file ] [ PubMed link ]

Islet 1 (Isl1) is a transcription factor of the LIM-homeodomain (LIM-HD) protein family. LIM-HD proteins all contain two protein-interacting LIM domains, a DNA-binding homeodomain (HD), and a C-terminal region. In Isl1, the C-terminal region also contains the LIM homeobox 3 (Lhx3)-binding domain (LBD), which interacts with the LIM domains of Lhx3. The LIM domains of Isl1 have been implicated in inhibition of DNA binding potentially through an intramolecular interaction with or close to the HD. Here we investigate the LBD as a candidate intramolecular interaction domain. Competitive yeast-two hybrid experiments indicate that the LIM domains and LBD from Isl1 can interact with apparently low affinity, consistent with no detection of an intermolecular interaction in the same system. Nuclear magnetic resonance studies show that the interaction is specific, whereas substitution of the LBD with peptides of the same amino acid composition but different sequence is not specific. We solved the crystal structure of a similar but higher affinity complex between the LIM domains of Isl1 and the LIM interaction domain from the LIM-HD cofactor protein LIM domain-binding protein 1 (Ldb1) and used these coordinates to generate a homology model of the intramolecular interaction that indicates poorer complementarity for the weak intramolecular interaction. The intramolecular interaction in Isl1 may provide protection against aggregation, minimize unproductive DNA binding, and facilitate cofactor exchange within the cell.

RbAp48 bound to MTA1(656-686)

[ PDB file ] [ PubMed link ]

RbAP48 and MTA1 are components of the Nucleosome Remodeling and Deacetylase (NuRD) complex. This structure provides a small step towards understanding how the complex is put together. Still plenty more to be done though!

RbAp48 bound to MTA1(670-695)

[ PDB file ] [ PubMed link ]

A second structure of the RbAp48-MTA1 subcomplex. A little bit more of MTA1 gave a substantially higher affinity, which can be rationalized in the structure by the formation of an additional hydrophobic cluster.

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