Structural highlights
Function
AT2A1_RABIT This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
Publication Abstract from PubMed
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.
Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.,Paulsen ES, Villadsen J, Tenori E, Liu H, Bonde DF, Lie MA, Bublitz M, Olesen C, Autzen HE, Dach I, Sehgal P, Nissen P, Moller JV, Schiott B, Christensen SB J Med Chem. 2013 May 9;56(9):3609-19. doi: 10.1021/jm4001083. Epub 2013 Apr 30. PMID:23574308[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Paulsen ES, Villadsen J, Tenori E, Liu H, Bonde DF, Lie MA, Bublitz M, Olesen C, Autzen HE, Dach I, Sehgal P, Nissen P, Moller JV, Schiott B, Christensen SB. Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase. J Med Chem. 2013 May 9;56(9):3609-19. doi: 10.1021/jm4001083. Epub 2013 Apr 30. PMID:23574308 doi:10.1021/jm4001083
