August 1, 1990Journal of Biological ChemistryOpen Access

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

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Structured PICO

Population

In vitro mutagenesis model of sarcoplasmic reticulum Ca2(+)-ATPase

Intervention

Mutations of conserved amino acids in the beta-strand domain (Thr181, Gly182, Glu183, Ser184, Asp157, Ser178, Asp149, Asp162, Gln177)

Comparator

Wild-type enzyme

Outcome

Ca2+ transport activity and conformational transition ratessurrogate

Conserved amino acids Thr181, Gly182, and Glu183 in the beta-strand domain of the sarcoplasmic reticulum Ca2+-ATPase are essential for the E1P to E2P conformational change during calcium transport.

Discussion

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Implication

Identifies SERCA residues critical for conformational change; leaves open therapeutic targeting in calcium-handling disorders.

Cite This Study

Clarke et al. (1990) studied this question.

synapsesocial.com/papers/6a7264fe75498292b70b8107 https://doi.org/10.1016/s0021-9258(18)77271-2

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

Structured PICO

Discussion

Implication

Cite This Study

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

Structured PICO

Discussion

Implication

Cite This Study

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