Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase

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Standard

Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase. / Skytte, Dorthe Mondrup; Møller, Jesper Vuust; Liu, Huizhen; Nielsen, Helle Østergren; Svenningsen, Louise Elsa; Jensen, Christina Mernøe; Olsen, Carl Erik; Christensen, Søren Brøgger.

I: Bioorganic & Medicinal Chemistry, Bind 18, Nr. 15, 2010, s. 5634-5646.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Skytte, DM, Møller, JV, Liu, H, Nielsen, HØ, Svenningsen, LE, Jensen, CM, Olsen, CE & Christensen, SB 2010, 'Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase', Bioorganic & Medicinal Chemistry, bind 18, nr. 15, s. 5634-5646. https://doi.org/10.1016/j.bmc.2010.06.032

APA

Skytte, D. M., Møller, J. V., Liu, H., Nielsen, H. Ø., Svenningsen, L. E., Jensen, C. M., Olsen, C. E., & Christensen, S. B. (2010). Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase. Bioorganic & Medicinal Chemistry, 18(15), 5634-5646. https://doi.org/10.1016/j.bmc.2010.06.032

Vancouver

Skytte DM, Møller JV, Liu H, Nielsen HØ, Svenningsen LE, Jensen CM o.a. Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase. Bioorganic & Medicinal Chemistry. 2010;18(15):5634-5646. https://doi.org/10.1016/j.bmc.2010.06.032

Author

Skytte, Dorthe Mondrup ; Møller, Jesper Vuust ; Liu, Huizhen ; Nielsen, Helle Østergren ; Svenningsen, Louise Elsa ; Jensen, Christina Mernøe ; Olsen, Carl Erik ; Christensen, Søren Brøgger. / Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase. I: Bioorganic & Medicinal Chemistry. 2010 ; Bind 18, Nr. 15. s. 5634-5646.

Bibtex

@article{32681cd0ba7811df825b000ea68e967b,
title = "Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase",
abstract = "Removal of each of the acyl groups of thapsigargin at O-3, O-8 and O-10 significant reduces the affinity of the inhibitors to the SERCA1a pump. Replacement of the acyl groups at O-3 and O-10 with flexible residues could be performed with only a minor decrease of the affinity, whereas introduction of voluminous stiff residues caused dramatic reduction of the affinity. The results can be rationalized on the basis of the interactions of thapsigargin with the SERCA1a pump as revealed from 3D X-ray structural models of thapsigargin bound to the SERCA1a. In conclusion the results confirm and elaborate the previously suggested pharmocophore model of thapsigargin.",
keywords = "Former LIFE faculty",
author = "Skytte, {Dorthe Mondrup} and M{\o}ller, {Jesper Vuust} and Huizhen Liu and Nielsen, {Helle {\O}stergren} and Svenningsen, {Louise Elsa} and Jensen, {Christina Mern{\o}e} and Olsen, {Carl Erik} and Christensen, {S{\o}ren Br{\o}gger}",
note = "Keywords: Thapsigargin; SERCA; Pharmacophore; Topography of binding cavity",
year = "2010",
doi = "10.1016/j.bmc.2010.06.032",
language = "English",
volume = "18",
pages = "5634--5646",
journal = "Bioorganic & Medicinal Chemistry",
issn = "0968-0896",
publisher = "Pergamon Press",
number = "15",

}

RIS

TY - JOUR

T1 - Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase

AU - Skytte, Dorthe Mondrup

AU - Møller, Jesper Vuust

AU - Liu, Huizhen

AU - Nielsen, Helle Østergren

AU - Svenningsen, Louise Elsa

AU - Jensen, Christina Mernøe

AU - Olsen, Carl Erik

AU - Christensen, Søren Brøgger

N1 - Keywords: Thapsigargin; SERCA; Pharmacophore; Topography of binding cavity

PY - 2010

Y1 - 2010

N2 - Removal of each of the acyl groups of thapsigargin at O-3, O-8 and O-10 significant reduces the affinity of the inhibitors to the SERCA1a pump. Replacement of the acyl groups at O-3 and O-10 with flexible residues could be performed with only a minor decrease of the affinity, whereas introduction of voluminous stiff residues caused dramatic reduction of the affinity. The results can be rationalized on the basis of the interactions of thapsigargin with the SERCA1a pump as revealed from 3D X-ray structural models of thapsigargin bound to the SERCA1a. In conclusion the results confirm and elaborate the previously suggested pharmocophore model of thapsigargin.

AB - Removal of each of the acyl groups of thapsigargin at O-3, O-8 and O-10 significant reduces the affinity of the inhibitors to the SERCA1a pump. Replacement of the acyl groups at O-3 and O-10 with flexible residues could be performed with only a minor decrease of the affinity, whereas introduction of voluminous stiff residues caused dramatic reduction of the affinity. The results can be rationalized on the basis of the interactions of thapsigargin with the SERCA1a pump as revealed from 3D X-ray structural models of thapsigargin bound to the SERCA1a. In conclusion the results confirm and elaborate the previously suggested pharmocophore model of thapsigargin.

KW - Former LIFE faculty

U2 - 10.1016/j.bmc.2010.06.032

DO - 10.1016/j.bmc.2010.06.032

M3 - Journal article

C2 - 20615710

VL - 18

SP - 5634

EP - 5646

JO - Bioorganic & Medicinal Chemistry

JF - Bioorganic & Medicinal Chemistry

SN - 0968-0896

IS - 15

ER -

ID: 21858685