... understanding life in molecular detail

Prof Tony North

Crystallography, Molecular Graphics, Biomolecular structure

My research interest has been in the use of X-ray crystallography and computational methods to study the structures and functions of molecules concerned with biological processes.

Current major projects include:

 

Structural studies have been concerned with the lipocalin family of proteins. Members of this family are involved in a wide range of biological phenomena, including the binding of pigments in insects and crustacea, the excretion of pheromones and the transport of vitamins and hormons in mammals. In collaboration with L. Sawyers group in Edinburgh, we have solved the structure of b-lactoglobulin. the major soluble protein from cows milk. The molecule is a dimer consisting of two identical subunits, each having the 8-stranded barrel typical of lipocalins. The b-barrel forms a pocket to transport a small, otherwise insoluble molecule (possibly vitamin A) from cow to calf.

The structures of two pheromone binding rodent urinary proteins, also members of the lipocalin family, have been solved recently. These proteins produced by male mice act as an attractant for females. A ribbon diagram of the mouse urinary protein is shown.

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Research Interests

Structural Studies of Lipocalins

Structural studies have been concerned with the lipocalin family of proteins. Members of this family are involved in a wide range of biological phenomena, including the binding of pigments in insects and crustacea, the excretion of pheromones and the transport of vitamins and hormons in mammals. In collaboration with L. Sawyers group in Edinburgh, we have solved the structure of b-lactoglobulin. the major soluble protein from cows milk. The molecule is a dimer consisting of two identical subunits, each having the 8-stranded barrel typical of lipocalins. The b-barrel forms a pocket to transport a small, otherwise insoluble molecule (possibly vitamin A) from cow to calf.

The structures of two pheromone binding rodent urinary proteins, also members of the lipocalin family, have been solved recently. These proteins produced by male mice act as an attractant for females. A ribbon diagram of the mouse urinary protein is shown.

Detailed research programme                  Close ▲

Selected Publications

  1. Blake, C.C.F., Mair. G.A., North. A.C.T., Phillips, D.C., and Sarma, V.R.,1967, "On the Conformation of the Hen Egg-white Lysozyme Molecule", Proc. Roy. Soc., B167, 365

  2. Barry, C D and North, A C T, 1971, “The use of a computer-controlled display system in the study of molecular conformations”, Cold Spring Harbor Symposia on Quantitative Biology, XXXVI, 577-584 

  3. Sansom C.E, North A.C.T. and Sawyer L., 1994 "Structural Analysis and Classification of Lipocalins and Related Proteins Using a Profile-search Method" Biochimica et Biophysica Acta 1208, 247-255.

  4. Flower D R, North A C T, Sansom C E, 2000, "The lipocalin protein family: structural and sequence  overview", Biochim Biophys Acta 1482(1-2),9-24,