Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of leucine 31 of phospholamban in structural and functional interactions with the Ca2+ pump of cardiac sarcoplasmic reticulum.

The Journal of biological chemistry - 18 Mar 2005

Chen Zhenhui, Stokes David L, Jones Larry R

Abstract excerpt

The ability of two loss-of-function mutants, L31A and L31C, of phospholamban (PLB) to bind to and inhibit the Ca(2+) pump of cardiac sarcoplasmic reticulum (SERCA2a) was investigated using a molecular cross-linking approach. Leu(31) of PLB, located at the cytoplasmic membrane boundary, is a critical amino acid shown previously to be essential for Ca(2+)-ATPase inhibition. We observed that L31A or L31C mutations...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Site
Share to Calcium-Transporting ATPases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cross-Linking Reagents

Share to Insecta

Share to Maleimides

Share to Microsomes

Share to Sarcoplasmic Reticulum

Share to Sarcoplasmic Reticulum Calcium-Transporting ATPases

Source

Identifiers

PMID: 15644311
DOI: 10.1074/jbc.M414007200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of leucine 31 of phospholamban in structural and functional interactions with the Ca2+ pump of cardiac sarcoplasmic reticulum.PMID 15644311Read ↗

Ca2+ binding to site I of the cardiac Ca2+ pump is sufficient to dissociate phospholamban.Semantic proximity Read ↗

Functional and physical competition between phospholamban and its mutants provides insight into the molecular mechanism of gene therapy for heart failure.Semantic proximity Read ↗

Sarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump.Semantic proximity Read ↗

Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Semantic proximity Read ↗

Mechanism of reversal of phospholamban inhibition of the cardiac Ca2+-ATPase by protein kinase A and by anti-phospholamban monoclonal antibody 2D12.Semantic proximity Read ↗

Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites.Semantic proximity Read ↗

Essential role for Pro21 in phospholamban for optimal inhibition of the Ca-ATPase.Semantic proximity Read ↗

Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump.Semantic proximity Read ↗

Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy.Semantic proximity Read ↗

Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human.Semantic proximity Read ↗

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.Semantic proximity Read ↗

A phospholamban-tethered cardiac Ca2+ pump reveals stoichiometry and dynamic interactions between the two proteins.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.