Wallace, Bonnie - Birkbeck, University of London - Department of Biological Sciences

研究领域

Structure and function of sodium channels My lab focuses on structure/function studies of membrane proteins and polypeptides, especially those involved in ion translocation and transport. Of particular interest are voltage-gated sodium channels: we have recently determined the first crystal structure of a sodium channel in its open conformation. We have also determined the first crystal structures of complex of a sodium channel with several eukaryotic sodium channel blockers, which we have shown (in collaboration with the Clapham Lab at Harvard) block prokaryotic channels, making this channel an excellent candidate for drug discovery/development. In the past, we have determined the crystal structures of the polypeptide ion channels such as antiamoebin, and trichtoxin (polypeptide antibiotics that act as ion channels). We have also developed a new chimeric approach for expression of membrane proteins, and have produced a functional 'minimal' sodium channel pore. Lab techniques My lab uses the techniques of X-ray crystallography and circular dichroism spectroscopy, cloning and expression, bioinformatics, and molecular modelling, as well as functional studies to examine structure/function relationships for ion channels. Protein Circular Dichroism Data Bank (PCDDB) In a collaborative project with R.W. Janes of Queen Mary, University of London, we have created the Protein Circular Dichroism Data Bank (PCDDB), a deposition and archiving data bank and associated validation software for circular dichroism spectra and the DichroMatch method for structural analyses. Research grants Our work is supported by grants from the BBSRC, the Wellcome Trust, the British Heart Foundation, and CNRS/The Royal Society.

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Bagneris, C., DeCaen, P.G., Naylor, C.E., Pryde, D., Nobeli, I., Clapham, D.E., & Wallace, B.A. (2014) The Prokaryotic NavMs Channel as a Structural and Functional Model for Eukaryotic Sodium Channel Antagonism. Proc. Natl. Acad. Sci. USA 111:.8428-8433. Kalsi, S. Powl, A.M. Wallace, B.A., Morgan, H., de Planque, M.R.R. (2014) Shaped apertures in photoresist films enhance the lifetime and mechanical stability of suspended lipid bilayers. Biophysical J 106:1650-1659. Assuero F. Garcia; Jose L.S. Lopes; Antonio J. Costa-Filho; B. A. Wallace, Ana P.U. Araujo. (2013) Membrane Interactions of Calgranulin C (S100A12). PLOSone 8:e82555. O’Reilly, A.O., Cole, A.R., Lopes, J.L.S., Lampert, A., Wallace, B.A. (2013) Chaperone-mediated native folding of a B-scorpion Toxin in the periplasm of Escherichia coli. BBA (General Subjects) 1840:10-15. Bagneris, C., DeCaen, P.G., Hall, B.A., Naylor, C.E., Clapham, D.E., Kay, C.W.M., Wallace, B.A. (2013) Role of the C-terminal domain in the structure and function of tetrameric sodium channels, Nature Communications 4:2645. Miles, A.J, Fedosova, N.U, Hoffmann, S.V., Wallace, B.A., Esmann, M. (2013) Stabilisation of Na,K-ATPase structure by the cardiotonic steroid ouabain. BBRC 435:300-305. Woollett, B., Whitmore, L., Janes, R.W., and Wallace, B.A. (2013) ValiDichro: a website for validating and quality control of protein circular dichroism spectra. Nucleic Acids Research 41:W417-421. Fernandez, D. I., Sani, M.–A., Miles, A. J, Wallace, B A, and Separovic, F. (2013) Membrane defects enhance the interaction of antimicrobial peptides, aurein 1.2 versus caerin 1.1. Biochimica et Biophysica Acta 1828: 1863–1872. Lopes, J.L.S., Orcia, D., Araujo, A.P.U., DeMarco, R., and Wallace, B.A.(2013) Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14). Biophysical Journal 104:2512-2520. D'Avanzo, N., McCusker, E.C., Powl, A.M., Miles, A.J., Nichols, C.G., and Wallace, B.A. (2013) Differential Lipid Dependence of the Function of Bacterial Sodium Channels. PLOSone 8: e61216. Ulmschneider, M.B., Bagneris, C., McCusker, E.C., DeCaen, P.G., Delling, M., Clapham, D.E., Ulmschneider, J.P. and Wallace, B.A. (2013) Molecular dynamics of ion transport through the open conformation of a bacterial voltage-gated sodium channel. Proc. Nat. Acad. Sci. USA 110, 6364-6369. Woollett, B., Klose, D., Cammack, R., Janes, R.W., and Wallace, B.A. (2012) JCAMP-DX for circular dichroism spectra and metadata. Pure and Applied Chemistry 84: 2171-2182. Janes, R.W., Miles, A.J., Woollett, B., Whitmore, L., Klose, D., and Wallace, B.A. (2012) Circular Dichroism Spectral Data and Metadata in the Protein Circular Dichroism Data Bank (PCDDB): A Tutorial Guide to Accession and Deposition. Chirality 24: 751-63. Klose, D., Wallace, B.A., and Janes, R.W. (2012) DichroMatch: A website for similarity searching of circular dichroism spectra. Nucleic Acids Res. 40:547-552. Powl, A.M., Miles, A.M., and Wallace, B.A. (2012) Transmembrane and extramembrane contributions to membrane protein thermal stability: studies with the nachbac sodium channel. Biochim. Biophys. Acta (Biomembranes) 1818:889-895. doi:10.1016/j.bbamem.2011.12.019. Erdmanis, L., O’Reilly, A.O., Williamson, M.S., Field, L.M., Turberg, A., and Wallace, B.A. (2012) Association of Neonicotinoid Insensitivity with a Conserved Residue in the Loop D Binding Region of the Tick Nicotinic Acetylcholine Receptor. Biochemistry 51: 4627-4629. O'Reilly, A.O., Eberhardt, E., Weidner, C., Alzheimer, C., Wallace, B.A., Lampert, A. 2012. Bisphenol A binds to the local anesthetic receptor site to block the human cardiac sodium channel. PLOS One 7:e41667 McCusker, E.C., Bagneris, C., Naylor, C.E., Cole, A.R., D'Avanzo, N., Nichols, C.G., and Wallace, B.A. (2012) Structure of a Bacterial Voltage-Gated Sodium Channel Pore Reveals Mechanisms of Opening and Closing. Nature Communications 3:1102. McCusker, E.C., D'Avanzo, N., Nichols, C.G., and Wallace, B.A. (2011) Simplified Bacterial "Pore" Provides Insight into the Assembly, Stability and Structure of Sodium Channels. J. Biol. Chem. 286:16386-16391. Whitmore, L., Woollett, B., Miles, A.J., Klose, D.P., Janes, R.W., and Wallace, B.A.(2011) PCDDB: The Protein Circular Dichroism Data Bank, A Repository for Circular Dichroism Spectral and Metadata. Nucleic Acids Research 39:D480-D486. Beich-Frandsen, M., Vecerek, B. Konarev, P.V., Sjoblom, B., Kloiber, K., Hammerle, H., Rajkowitsch, L., Miles, A.J., Kontaxis, G., Wallace, B.A., Svergun, D.I., Konrat, R., Blasi, U. and Djinovic-Carugo, K. (2011) Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. Nucleic Acids Research , 39:4900-4915. Wallace, B.A., Gekko, K., Hoffmann, S.V., Lin, Y-H.,Sutherland, J.C., Tao, Y., Wien, F., and Janes, R.W. (2011) Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy - An Emerging Method in Structural Biology for Examining Protein Conformations and Protein Interactions. Nuclear Instrumentation and Methods A 649: 177-178. Moore, B.,Miles, A.J., Guerra-Giraldez, C., Simpson, P., Iwata, M., Wallace, B.A., Matthews,S.J., Smith, D.F., and Brown, K.A. (2011) Structural Basis of Molecular Recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane Surfaces. J. Biol. Chem. 286:9246-9256.