Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase
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Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase. / Paulsen, Eleonora Sandholdt; Villadsen, Jesper; Tenori, Eleonora; Liu, Huizhen; Bonde, Ditte Fast; Lie, Mette Alstrup; Bublitz, Maike; Olesen, Claus Linding; Autzen, Henriette Elizabeth; Dach, Ingrid; Sehgal, Pankaj; Nissen, Poul; Møller, Jesper; Schiøtt, Birgit; Christensen, S Brøgger.
I: Journal of Medicinal Chemistry, Bind 56, Nr. 9, 09.05.2013, s. 3609-19.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › fagfællebedømt
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TY - JOUR
T1 - Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase
AU - Paulsen, Eleonora Sandholdt
AU - Villadsen, Jesper
AU - Tenori, Eleonora
AU - Liu, Huizhen
AU - Bonde, Ditte Fast
AU - Lie, Mette Alstrup
AU - Bublitz, Maike
AU - Olesen, Claus Linding
AU - Autzen, Henriette Elizabeth
AU - Dach, Ingrid
AU - Sehgal, Pankaj
AU - Nissen, Poul
AU - Møller, Jesper
AU - Schiøtt, Birgit
AU - Christensen, S Brøgger
PY - 2013/5/9
Y1 - 2013/5/9
N2 - A crystal structure suggests four water molecules are present in the binding cavity of thapsigargin in sarco/endoplasmic reticulum calcium ATPase (SERCA). Computational chemistry indicates that three of these water molecules mediate an extensive hydrogen-bonding network between thapsigargin and the backbone of SERCA. The orientation of the thapsigargin molecule in SERCA is crucially dependent on these interactions. The hypothesis has been verified by measuring the affinity of newly synthesized model compounds, which are prevented from participating in such water-mediated interactions as hydrogen-bond donors.
AB - A crystal structure suggests four water molecules are present in the binding cavity of thapsigargin in sarco/endoplasmic reticulum calcium ATPase (SERCA). Computational chemistry indicates that three of these water molecules mediate an extensive hydrogen-bonding network between thapsigargin and the backbone of SERCA. The orientation of the thapsigargin molecule in SERCA is crucially dependent on these interactions. The hypothesis has been verified by measuring the affinity of newly synthesized model compounds, which are prevented from participating in such water-mediated interactions as hydrogen-bond donors.
U2 - 10.1021/jm4001083
DO - 10.1021/jm4001083
M3 - Journal article
C2 - 23574308
VL - 56
SP - 3609
EP - 3619
JO - Journal of Medicinal Chemistry
JF - Journal of Medicinal Chemistry
SN - 0022-2623
IS - 9
ER -
ID: 45874326