Allosteric modulation of the sarcoplasmic reticulum Ca2+ATPase by thapsigarginviadecoupling of functional motions-Reference-Cited by-同舟云学术

Allosteric modulation of the sarcoplasmic reticulum Ca2+ATPase by thapsigarginviadecoupling of functional motions

Published:2019 Issue:39 Volume:21 Page:21991-21995
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Saleh Noureldin¹²³⁴⁵^ORCID,Wang Yong¹²³⁴⁵^ORCID,Nissen Poul⁶⁷⁸⁵^ORCID,Lindorff-Larsen Kresten¹²³⁴⁵^ORCID

Affiliation:

1. Linderstrøm-Lang Centre for Protein Science

2. Dept. of Biology

3. University of Copenhagen

4. Copenhagen

5. Denmark

6. DANDRITE – Nordic EMBL Partnership for Molecular Medicine and Department of Molecular Biology and Genetics

7. Aarhus University

8. Aarhus

Abstract

Thapsigargin binding to the Ca²⁺-ATPase SERCA induces a conformational change in the transmembrane regions without regulation of the cytoplasmic domains, and causes a conformational change in the cytoplasmic domains uncoupled from nucleotide binding.

Funder

Lundbeckfonden

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP04736K

Reference37 articles.

1. In and out of the cation pumps: P-Type ATPase structure revisited

2. Inhibition of the sarcoplasmic reticulum Ca2+ transport ATPase by thapsigargin at subnanomolar concentrations

3. Engineering a Prostate-Specific Membrane Antigen–Activated Tumor Endothelial Cell Prodrug for Cancer Therapy