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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 - 65] [66 - 69]
Point mutant of the third zinc finger of BKLF

[ PDB file ]

This protein is tryptophan-containing mutant of BKLF F3 that retains native structure and function. The addition of tryptophan enables the use of fluorescence spectroscopy for conducting folding studies.

Extension mutant of the third zinc finger of BKLF

[ PDB file ]

This structure shows a two-residue insertion mutant of BKLF F3 that possesses native function but not native structure. This zinc finger retains the ability to bind to GATA-1, even though it contains two additional bulky residues in a structurally important region.

Antifreeze protein from an Antarctic fish

[ PDB file ] [ PubMed link ]

Many animals that live in extremely cold climates produce proteins that act to prevent the formation of ice crystals in the bodily fluids of the organism. Antarctic fish produce a range of such proteins, as the water temperatures can drop below 0 degrees Celsius. We have determined the structure of the type I antifreeze protein (SS3) from the blood of the shorthorn sculpin at both 5 degrees and -5 degrees. The structure largely comprises a long alpha-helix that displays conserved Thr residues (red) along a single surface. These residues are important for preventing the growth of ice crystals, although the mechanism of action is not currently understood. An additional short helix exists at the N-terminus of the protein, although the conformational relationship between the two helices is not well defined. This is the first solution structure of a wild-type type I antifreeze protein.

SS3 antifreeze protein at -5 degrees

[ PDB file ] [ PubMed link ]

In order to get an idea of the conformation of SS3 at a sub-zero temperature, we determined the structure of SS3 at -5 degrees Celcius. Getting the solution down to that temperature without freezing was straighforward - slow cooling together with the salt present in the buffer (~50 mM phosphate) does the trick. No dramatic changes were observed - the structure comprised a large and a small helical region, connected by a short, slightly less well defined sequence.

Stripped down CHANCE domain #1

[ PDB file ] [ PubMed link ]

This is a minimalised version of the CHANCE domain. 12 of the 25 residues have been mutated (mostly to alanine), but the fold is retained. This 'stripping down' of the surface of the domain is the first step in re-designing the domain to have new binding functionality. This structure contains ~50% Ala and has a very similar fold to the wild type sequence, indicating that zinc-ligands and a few key hydrophobic residues are all that is required for structure.

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