 |
PDBsum entry 4j2t
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/hydrolase inhibitor
|
PDB id
|
|
|
|
4j2t
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Water-Mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.
|
|
|
Authors
|
|
E.S.Paulsen,
J.Villadsen,
E.Tenori,
H.Liu,
D.F.Bonde,
M.A.Lie,
M.Bublitz,
C.Olesen,
H.E.Autzen,
I.Dach,
P.Sehgal,
P.Nissen,
J.V.Møller,
B.Schiøtt,
S.B.Christensen.
|
|
|
Ref.
|
|
J Med Chem, 2013,
56,
3609-3619.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
