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Structure and Regulation of of Small G Proteins and their effectors

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  • Full or part time
    Dr Mott
  • Application Deadline
    No more applications being accepted
  • Funded PhD Project (European/UK Students Only)
    Funded PhD Project (European/UK Students Only)

Project Description

BBSRC funded Industrial CASE Partnership Studentship with AstraZeneca.

Applications are invited for a BBSRC-funded 4-year PhD studentship starting October 2016 in a collaborative project between Dr Helen Mott in the Department of Biochemistry and Dr Sarah Ross and Dr Nichola Whalley in the Oncology group at AstraZeneca. The project involves an investigation of the small G protein RalA and its interaction with membranes using biochemical, biophysical and NMR based approaches in the Mott lab. RalA variants will be generated and their effect on RalA function will be tested in cancer cell lines at the AstraZeneca labs in Cambridge. The studentship will pay all EU/UK fees, an enhanced stipend and a contribution to attendance at conferences. Enthusiastic students with at least a good 2.i or 1st class degree (or equivalent) in Biochemistry or a related subject are encouraged to apply. We particularly welcome applicants who are interested in learning structural biology alongside functional assays and will relish the opportunity to experience research in both the academic and industrial setting. The techniques that the student will learn include: molecular biology, protein purification, NMR and fluorescence spectroscopy, CRISPR and mammalian tissue culture.

Applications should be sent to Helen Mott ([email protected]), including a CV detailing academic achievements so far, a motivational statement and the names and contact details of two referees.

Funding Notes

BBSRC funding is available for UK nationals and EU students who meet the residency requirements. Further information about eligibility for funding can be found on the BBSRC website:
http://www.bbsrc.ac.uk/documents/studentship-eligibility-pdf/

References

R.B. Fenwick, L.J. Campbell, K. Rajasekar, S. Prasannan, D. Nietlispach, J. Camonis D. Owen, H.R. Mott (2010) The RalB-RLIP76 complex reveals a novel mode of Ral-effector interaction. Structure 18 985-995.
K.V. Rajasekar, L.J. Campbell, D. Nietlispach, D. Owen & H.R. Mott (2013) The structure of the RLIP76 (RalBP1) RhoGAP domain-Ral binding domain dyad: fixed position of the domains leads to dual engagement of small G proteins at the membrane. Structure 21 2131-2142.
C. L. Hutchinson, P.N. Lowe, S.H. McLaughlin, H.R. Mott & Owen D (2013). Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB. Biochemistry. 52 7999-8011
L. J Campbell, M. Peppa, M.D. Crabtree, A. Shafiq, N.F. McGough, H.R. Mott & D. Owen (2015) Thermodynamic mapping of effector protein interfaces with RalA and RalB. Biochemistry. 54 1380-1389
H.R. Mott & D. Owen (2015) Structures of Ras superfamily effector complexes: What have we learnt in two decades? Crit Rev Biochem Mol Biol. 50 85-133.

How good is research at University of Cambridge in Biological Sciences?

FTE Category A staff submitted: 189.63

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