ArticleProteins2015
Evaluation of conformational changes in diabetes-associated mutation in insulin a chain: a molecular dynamics study.
Article in Proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- A Review of the Biosynthesis and Structural Implications of Insulin Gene Mutations Linked to Human Disease.Cells · 2023Review
- Progress in Simulation Studies of Insulin Structure and Function.Frontiers in endocrinology · 2022Review
- Article
- The metastable states of proteins.Protein science : a publication of the Protein Society · 2020Review
- Molecular dynamics simulations revealed structural differences among WRKY domain-DNA interaction in barley (Hordeum vulgare).BMC genomics · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Insulin plays a central role in the regulation of metabolism in humans. Mutations in the insulin gene can impair the folding of its precursor protein, proinsulin, and cause permanent neonatal-onset diabetes mellitus known as Mutant INS-gene induced Diabetes of Youth (MIDY) with insulin deficiency. To gain insights into the molecular basis of this diabetes-associated mutation, we perform molecular dynamics simulations in wild-type and mutant (Cys(A7) to Tyr or C(A7)Y) insulin A chain in aqueous solutions. The C(A7)Y mutation is one of the identified mutations that impairs the protein folding by substituting the cysteine residue which is required for the disulfide bond formation. A comparative analysis reveals structural differences between the wild-type and the mutant conformations. The analyzed mutant insulin A chain forms a metastable state with major effects on its N-terminal region. This suggests that MIDY mutant involves formation of a partially folded intermediate with conformational change in N-terminal region in A chain that generates flexible N-terminal domain. This may lead to the abnormal interactions with other proinsulins in the aggregation process.
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Registered trials
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