TY  - JOUR
AU  - Rossetti, Giulia
AU  - Dibenedetto, Domenica
AU  - Calandrini, Vania
AU  - Giorgetti, Alejandro
AU  - Carloni, Paolo
TI  - Structural predictions of neurobiologically relevant G-protein coupled receptors and intrinsically disordered proteins
JO  - Archives of biochemistry and biophysics
VL  - 582
SN  - 0003-9861
CY  - San Diego, Calif.
PB  - Elsevier
M1  - FZJ-2015-03626
SP  - 91–100
PY  - 2015
N1  - .
AB  - G protein coupled receptors (GPCRs) and intrinsic disordered proteins (IDPs) are key players for neuronal function and dysfunction. Unfortunately, their structural characterization is lacking in most cases. From one hand, no experimental structure has been determined for the two largest GPCRs subfamilies, both key proteins in neuronal pathways. These are the odorant (450 members out of 900 human GPCRs) and the bitter taste receptors (25 members) subfamilies. On the other hand, also IDPs structural characterization is highly non-trivial. They exist as dynamic, highly flexible structural ensembles that undergo conformational conversions on a wide range of timescales, spanning from picoseconds to milliseconds. Computational methods may be of great help to characterize these neuronal proteins. Here we review recent progress from our lab and other groups to develop and apply in silico methods for structural predictions of these highly relevant, fascinating and challenging systems.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000360781200010
C6  - pmid:25797436
DO  - DOI:10.1016/j.abb.2015.03.011
UR  - https://juser.fz-juelich.de/record/201329
ER  -