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Article

Functional consequences of mutations of conserved amino acids in the beta-strand domain of the Ca2(+)-ATPase of sarcoplasmic reticulum.

The Journal of biological chemistry - 25 Aug 1990

Clarke D M, Loo T W, MacLennan D H

Abstract excerpt

The sequences Thr-Gly-Glu-Ser184 and Asp-Gln-Ser178 and individual residues Asp149, Asp157, and Asp162 in the sarcoplasmic reticulum Ca2(+)-ATPase are highly conserved throughout the family of cation-transporting ATPases. Mutant Thr181----Ala, Gly182----Ala, Glu183----Ala, and Glu183----Gln, created by in vitro mutagenesis, were devoid of Ca2+ transport activity. None of these mutations, however, affected...

Topics

Amino Acid Sequence
Animals
Calcium-Transporting ATPases
Cell Line
Codon
Kinetics
Macromolecular Substances
Microsomes
Molecular Sequence Data
Muscles
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligonucleotide Probes

Phosphorylation

Rabbits

Sarcoplasmic Reticulum

Transfection

Source

Identifiers

PMID: 2143758

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2143758-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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