Oxford University, Structural Bioinformatics & Computational Biochemistry Unit
Home  |  Mission  |  Research  |  Members  |  Positions  |  Image Gallery  |  Panoramas  |  Seminars
Databases: Bookshelf · CGDB · KDB · OMPDB · Lipidbook  |  Links  |  Contact  |  Intranet  |  Search
 

Craig Lumb


Structural Bioinformatics and Computational Biochemistry Unit
Department of Biochemistry
University of Oxford
South Parks Road
Oxford
OX1 3QU
UK

Telephone: 01865 613304
Fax: 01865 613238

e-mail: craig.lumb@bioch.ox.ac.uk
division line

Computational studies of signalling at the cell membrane


Background


I read Natural Sciences at St. John's College, Cambridge between October 2004 and June 2008. For my undergraduate research project in my final year I worked with Dr Mark Miller in the Theory Sector of the Department of Chemistry, using molecular dynamics simulations to study the behaviour and topological characteristics of low density dipolar colloidal gels.

In October 2008 I moved to Merton College, Oxford for a DPhil with Professor Mark Sansom in the Structural Bioinformatics and Computational Biochemistry Unit, supported by the Medical Research Council. I successfully defended my DPhil thesis in October 2012.



Research


Cell signalling pathways are crucial for many biological processes including cell proliferation and survival. Signalling is governed by a complex network of interactions within the cell, and disruption of signalling can lead to a variety of human diseases such as cancer. Often, a key event in the signalling cascade is the reversible recruitment of peripheral membrane proteins to the surface of the cytoplasmic leaflet of the cell membrane. These proteins have a variety of functions at the membrane surface and are involved in membrane-mediated protein-protein and protein-ligand interactions essential for subsequent downstream signalling. Protein-membrane association is achieved with the aid of a comparatively rare class of negatively charged lipids called the phosphoinositides (PIs), which are thought to recruit cytosolic proteins to the membrane through electrostatic interactions. We are currently studying several of these PI-binding proteins using a variety of modelling and simulation techniques in an effort to understand how they interact with the membrane. We also collaborate with a number of experimental research groups in the UK and in the USA:


Publications


  1. Craig N. Lumb and Mark S. P. Sansom
    Defining the membrane associated state of the PTEN tumor suppressor protein
    Biophysical Journal (2013) 104 613-621

  2. Luke A. Yates, Craig N. Lumb, Nina N. Brahme, Ruta Zalyte, Louise E. Bird, Luigi De Colibus, Raymond J. Owens, David A. Calderwood, Mark S. P. Sansom and Robert J. C. Gilbert
    Structural and functional characterisation of the kindlin-1 pleckstrin homology domain
    Journal of Biological Chemistry (2012) 287 43246-43261

  3. Craig N. Lumb and Mark S.P. Sansom
    Finding a needle in a haystack: The role of electrostatics in target lipid recognition by PH domains
    PLoS Computational Biology (2012) 8 e1002617

  4. Mostyn T. Brown, Bradley C. Steel, Claudio Silvestrin, David A. Wilkinson, Nicolas J. Delalez, Craig N. Lumb, Boguslaw Obara, Judith P. Armitage and Richard M. Berry
    Flagellar hook flexibility is essential for bundle formation in swimming Escherichia coli cells
    Journal of Bacteriology (2012) 194 3495-3501

  5. Craig N. Lumb, Ju He, Yi Xue, Phillip J. Stansfeld, Robert V. Stahelin, Tatiana G. Kutateladze and Mark S.P. Sansom
    Biophysical and computational studies of membrane penetration by the GRP1 pleckstrin homology domain
    Structure (2011) 19 1338-1346

  6. Mark A. Miller, Ronald Blaak, Craig N. Lumb and Jean-Pierre Hansen
    Dynamical arrest in low density dipolar colloidal gels
    Journal of Chemical Physics (2009) 130 114507



Or search publications using PubMed


A copy of my DPhil thesis has been deposited in the Oxford University Research Archive.


Conference Presentations



Last updated 07/09/11