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Structural Biology 2018
Volume: 4
Biochemistry & Molecular Biology Journal
Page 46
March 15-16 2018
Barcelona, Spain
10
th
Edition of International Conference on
Structural Biology
S
TIM1 serves as calcium sensor protein in the endoplasmic
reticulum of the cell which extends into the cytosol and
oligomerises upon calcium store depletion. The cytosolic part
of STIM1 consists of one long and two short coiled coil domains
directly involved in homo-oligomerization leading to spatial
elongation of the STIM1 protein and activation of the Orai calcium
channel. The Stormorken syndrome associated with a single
point mutation (R304W) within this region of STIM1 results in
permanent activation of Orai channel. Using high resolution
solution state NMR we have found a helix elongation within the
short coiled coil domain of the mutant close to the mutation
position with respect to the wild type STIM1. These findings
corroborate the increased propensity of this domain to form
homomers destabilizing the resting state of STIM1, which leads
to the increased channel activation.
Biography
Petr Rathner has completed his Double Degree Mgr/MSc in 2013 from Jo-
hannes Kepler University of Linz (Austria) and University of South Bohemia
(Czech Republic). Currently, he is a PhD student in the group of Professor
Norbert Müller Nanocell research (JKU Linz, Austria) focusing on biomolec-
ular nuclear magnetic resonance spectroscopy.
petr.rathner@jku.atStormorken syndrome disease STIM1 protein studied by high
resolution NMR
Petr Rathner
a
, Michael Stadlbauer
b
, Linda Cerofolini
c
, Enico Ravera
c
, Marc Fahrner
b
, Lukas Traxler
b
, Claudio Luchinat
c
, Christoph Romanin
b
and
Norbert Müller
a,d
a
Johannes Kepler University Linz, Austria
b
Johannes Kepler University Linz, Austria
c
Magnetic Resonance Center, Italy
d
University of South Bohemia, Czech Republic
Petr Rathner et al., Biochem Mol biol J, Volume 4
DOI: 10.21767/2471-8084-C1-009