2 O T 2 P N N S I D E N T ' S
M E E T I N G
CHRnTTCES IN BIOMOLECULAR MODELING - FRoM QM rO CoARSE'GRAINING
LANcuoluBN, StocxHol,irl, SwnlnN, 17 -20 fuNE 2012
I
ORcRtrltznRs
Lennart Nilsson, President ISQBP, Karolinska Institutet Alessandra Villa, Karolinska Insitutet
Fahmi Himo, Stockholm University
Meeting coordinator
Monica Ahlberg, Karolinska Institutet
Wenner-Gren Stiftelserna
ttle nner-Ere n Fou ndatians
\r
fl
Vetenskapsridet
UruIBRELLA
SAMPLEIUG
CALEUTATIOT{S
OF TI.IE
Bf NDING
FREE
ENER.GV
[N TH{E
UVRE
EIfr4ER
Min Wua, Ake Strido and Leif A. Erikssona
uschool of Chemistry and Molecular Biology, IJniversity of Gothenburg, SE-41296, Gdteborg, Sweden
bschool of Science and Technology, Orebro lJniversity, SE-70182 6rebro, Sweden
min.wu@chem.gu.se
The dimeric {JVR.B protein is a ultraviolet-B radiation (280-315 nm) photoreceptor that is responsible for the first step in tlV-ts regulation of gene expression in plantst. Xtr action comprises the actual absorption of the {JV quanta by a Trp affay in the protein, followed by monomerisation, and subsequent aggregation with downstream signaling components2. A crystal structure of the Arabidopsis thaliana tryptophan-rich wild type U\IR.B protein dimer was published. IJmbrella sampling method was used to calculate the binding free energy for the wild type IJVRB dimer and three of its mutants (R.286A, R338,{ and R2B6A/R.33BA), in order to veriff the key mutants able to disrupt the dimeric structure.
Referemces"
[1] Brown BA, Cloxi C, Jiang GH, Kaiserli E, Herzyk P, Kliebenstein DJ, Jenkins G1,.2005. A UV-B-specific singaling component orchestrates plant UV protection. Proc. Natl.Acad.sci.USA 102:18225-30.
[2] Rizzini L, Favory JJ, Cloix C, Faggionato D, Hara AO, Kaiserli E, Baumeister R, Schiifer E, Nagy F, Jenkins Gl, Ulm R. 20't{. Perception of UV-B by the Arabidopsis UVRB protein. Science 332:103-107.
