| Structural highlights
4j2t is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 3nal, 3nan, 3nam, 2c8k, 3n5k |
| Activity: | Calcium-transporting ATPase, with EC number 3.6.3.8 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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.
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
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