Abstract
Background: Phospholamban (PLB) regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) activity and is thus a key regulator of cardiac contractility. Results: We present the crystal structure of SERCA in complex with PLB at 2.8-A resolution. Conclusion: PLB stabilizes a divalent cation-free conformation of SERCA with collapsed Ca2+ binding sites. We call the structure E2-PLB. Significance: The E2-PLB structure explains how PLB decreases Ca2+ affinity and depresses cardiac contractility.
Original language | English |
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Pages (from-to) | 30181-30191 |
Number of pages | 11 |
Journal | Journal of Biological Chemistry |
Volume | 288 |
Issue number | 42 |
DOIs | |
State | Published - Oct 18 2013 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
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The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. / Akin, Brandy L.; Hurley, Thomas; Chen, Zhenhui; Jones, Larry.
In: Journal of Biological Chemistry, Vol. 288, No. 42, 18.10.2013, p. 30181-30191.Research output: Contribution to journal › Article
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TY - JOUR
T1 - The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum
AU - Akin, Brandy L.
AU - Hurley, Thomas
AU - Chen, Zhenhui
AU - Jones, Larry
PY - 2013/10/18
Y1 - 2013/10/18
N2 - Background: Phospholamban (PLB) regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) activity and is thus a key regulator of cardiac contractility. Results: We present the crystal structure of SERCA in complex with PLB at 2.8-A resolution. Conclusion: PLB stabilizes a divalent cation-free conformation of SERCA with collapsed Ca2+ binding sites. We call the structure E2-PLB. Significance: The E2-PLB structure explains how PLB decreases Ca2+ affinity and depresses cardiac contractility.
AB - Background: Phospholamban (PLB) regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) activity and is thus a key regulator of cardiac contractility. Results: We present the crystal structure of SERCA in complex with PLB at 2.8-A resolution. Conclusion: PLB stabilizes a divalent cation-free conformation of SERCA with collapsed Ca2+ binding sites. We call the structure E2-PLB. Significance: The E2-PLB structure explains how PLB decreases Ca2+ affinity and depresses cardiac contractility.
UR - http://www.scopus.com/inward/record.url?scp=84885968069&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84885968069&partnerID=8YFLogxK
U2 - 10.1074/jbc.M113.501585
DO - 10.1074/jbc.M113.501585
M3 - Article
C2 - 23996003
AN - SCOPUS:84885968069
VL - 288
SP - 30181
EP - 30191
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 42
ER -