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March 1, 1996Journal of Biological ChemistryOpen Access

A Leucine Zipper Stabilizes the Pentameric Membrane Domain of Phospholamban and Forms a Coiled-coil Pore Structure

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Population

Phospholamban protein (specifically amino acid residues 26-52 of the channel-forming domain)

Design

Preclinical

Authors

HSHeather K.B. SimmermanAmgen (United States)YKYvonne M. KobayashiEli Lilly (United States)JAJoseph M. AutryUniversity of Maryland, Baltimore

Discussion

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Overview

Preclinical mapping of phospholamban leucine zipper residues informs future mutagenesis; leaves open effects on cardiac calcium handling in vivo.

Structured PICO

P
Population
Phospholamban protein (specifically amino acid residues 26-52 of the channel-forming domain)
I
Intervention
Mutational analysis (individual mutation of residues 26-52 to Ala or Phe)
O
Outcome
Ability of the mutant to form a pentamer or other oligomer assessed by SDS-polyacrylamide gel electrophoresissurrogate

Identifies specific amino acid residues forming a leucine zipper motif that is essential for stabilizing the pentameric membrane domain of phospholamban.

Cite This Study

Simmerman et al. (1996) studied this question.

synapsesocial.com/papers/6a75a3f6ef3d015f2ddd7f72https://doi.org/10.1074/jbc.271.10.5941
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins1988 · 3,518 citations
  2. 2Comparative studies of cardiac and skeletal sarcoplasmic reticulum ATPases. Effect of a phospholamban antibody on enzyme activation by Ca2+1993 · 166 citations
  3. 3Phospholamban forms Ca2+-selective channels in lipid bilayers.1988 · 140 citations
  4. 4Empirical Predictions of Protein Conformation1978 · 3,145 citations
  5. 5Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.1994 · 168 citations