What is it about?
Replacement of Histidine98 with a Tyrosine induces the onset of myoglobinopathy, a rare autosomal dominant myopathy, featuring highly characteristic sarcoplasmic inclusions in skeletal and cardiac muscle. The disease manifests in adulthood with proximal and axial muscle weakness and progresses to cause wheel-chair dependence and respiratory and cardiac failure. In this paper, we characterize the effect of the His98Tyr mutation on the reactivity of myoglobin to unravel the molecular mechanism(s) leading to the disease and its progressive evolution.
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Why is it important?
Understanding the molecular basis of myoglobinopathy is relevant to the development of strategies to slow down or inhibit its progression. The effects of the His98Tyr mutation on the reactivity of myoglobin result from from bond formation/cleavage events occurring at the distal and proximal heme sites, suggesting that the molecular determinants of myoglobin are localized there.
Perspectives
the findings reported in the paper set the basis for clarifying the onset of the cascade of chemical events that are responsible for the pathological symptoms of myoglobinopathy.
PhD Gianantonio Battistuzzi
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia
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This page is a summary of: Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy, European Journal of Biochemistry, November 2021, Wiley,
DOI: 10.1111/febs.16235.
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