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Home > Learning > Departments > Institute of Molecular Biosciences > Staff > sutherland-smith_andrew

Institute of Molecular Biosciences

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sutherland-smith.jpg Dr Andrew Sutherland-Smith
Senior Lecturer in Structural Biology

Address:

Institute of Molecular BioSciences,
Massey University, Private Bag 11222,
Palmerston North New Zealand

Phone:

+64 6 350 5515 extn:-2578

Fax

+64 6 350 5688

Email:

A.J. Sutherland-Smith@massey.ac.nz


Background

B.Sc. (Hons) and Ph.D., Massey University.
Post-doctoral fellow, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK

Research Interests

  • Protein structure and function

  • Inherited diseases

  • The cytoskeleton

  • Muscle and bone development

More information is available on Andrew's lab website.

Selected Publications

  • Sutherland-Smith, A.J.  (2011) Filamin structure, function and mechanics: Are altered filamin mediated force responses associated with human disease? Biophysical Reviews 3, 15-23
    .
  • Starck, C.S. & Sutherland-Smith, A.J. (2010) Amyloid formation by the myostatin precursor protein. PLoS One, 5, e9170.

  • Sawyer, G.M., Clark, A.R., Robertson, S.P. & Sutherland-Smith, A.J. (2009) Disease-associated Substitutions in the Filamin B Actin-binding Domain Confer Enhanced Actin Binding Affinity in the Absence of Major Structural Disturbance: Insights from the Crystal Structure of Filamin B Actin-binding Domains. Journal of Molecular Biology 390, 1030-1047.

  • Roberts, R.C., Sutherland-Smith, A.J., Wheeler, M.A., Norregaard Jensen, O., Emerson, L.J., Spiliotis, I.I., Tate, C.G., Kendrick-Jones, J. and Ellis, J.A. (2006). The Emery-Dreifuss Muscular Dystrophy associated-protein emerin is protein kinase A-dependently phosphorylated on serine 49. FEBS Journal, 273, 4562-4575.

  • Hamed, S., Sutherland-Smith, A., Gorospe, J., Kendrick-Jones, J. and Hoffman, E. (2005). DNA sequence analysis for structure/function and mutation studies in Becker muscular dystrophy. Clinical Genetics, 68, 69-79.

  • Lehman, W., Craig, R., Kendrick-Jones, J. and Sutherland-Smith, A.J. (2004). An open or closed case for the conformation of calponin homology domains on F-actin. Journal of Muscle Research and Cell Motility, 25, 351-358.

  • Sutherland-Smith, A.J., Moores, C.A., Norwood, F.L.M., Hatch, V., Craig, R., Kendrick-Jones, J. and Lehman, W. (2003). An atomic model for actin-binding by the CH-domains and spectrin-repeat modules of utrophin and dystrophin. Journal of Molecular Biology, 329, 15-33.

  • Robertson, S.P., Twigg, S.R.F., Sutherland-Smith, A.J., Biancalana, V., Gorlin, R.J., Horn, D., Kenwrick, S.J., Kim, C.A., Morava, E., Newbury-Ecob, R., Ørstavik, K.H., Quarrell, O., Schwartz, C., Shears, D.J., Suri, M., Kendrick-Jones, J., The OPD-spectrum Disorders Clinical Collaborative Group and Wilkie, A.O.M. (2003). Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans. Nature Genetics, 33, 487-491.

  • Norwood, F.L.M., Sutherland-Smith, A.J., Keep, N.H. and Kendrick-Jones, J. (2000). Crystal structure of the N-terminal actin-binding domain of dystrophin and implications for Duchenne muscular dystrophy. Structure, 8, 481-491.

  • Sutherland-Smith, A.J., Baker, H.M., Hofmann, O.M., Brittain, T. and Baker, E.N. (1998). Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of Gower II (a2e2) haemoglobin at 2.9 Å resolution. Journal of Molecular Biology, 280, 475-484.

  • Baker, E.N., Anderson, B.F., Baker, H.M., Faber, R., Smith, C.A. and Sutherland-Smith, A.J. (1997). Structural and functional flexibility of lactoferrin. In Lactoferrin Interactions and Biological Functions. Edited by H.T. William and B. Lönnerdal, Humana, Totowa, NJ, 177-191.

  • Smith, C.A., Sutherland-Smith, A.J., Kepler, B.K., Kratz, F. and Baker, E.N. (1996). Binding of ruthenium(III) anti-tumor drugs to human lactoferrin probed by high resolution X-ray crystallographic structure analyses. Journal of Biological Inorganic Chemistry, 1, 424-431.

Page authorised by HOI, Institute of Molecular BioSciences
Last updated on Friday 09 March 2012

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