11 October 2013

Using Nuclear Magnetic Resonance (NMR) to Study Protein Function in Cancer and Infection

Organised by:

SCI's Biotechnology Group in conjunction with the University of Westminster

University of Westminster

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Synopsis

Protein NMR spectroscopy allows the determination of protein structure, dynamics and
interactions with ligands or other proteins. This talk describes pieces of work underway in Dr
Blumenschein's research group at the University of East Anglia, applying protein NMR to
different problems. ADAM-15 is a transmembrane protein with a large extracellular domain
and a small intracellular domain, subject to alternative splicing. Different isoforms of the
cytoplasmic domain are associated with different prognosis in breast cancer, and this is
believe to be due to different interactions with SH3 domains of signalling kinases. We are
using NMR to look at how the different isoforms interact with the kinases. Tarp (translocated
actin recruiting protein) is an intrinsically disordered protein from Chlamydia involved in host
cell invasion. In the initial stages of infection, the effector Tarp is injected into the host cell,
where it nucleates the formation of actin filaments. Using NMR and other biophysical
techniques, we have been looking at the interaction between Tarp and actin, and how Tarp
changes its secondary structure upon binding. The last example is Avr3a11, an effector from
a plant pathogen, Phytophthora capsicii. We have used NMR to determine the solution
structure of the effector domain from Avr3a11 and study its dynamics.