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Article

The B22 Dilemma: Structural Basis for Conformational Differences in Proinsulin B-Chain Arg22 Mutants.

Biomolecules - 12 Apr 2025

Ranganathan Srivastav, Arunagiri Anoop

Abstract excerpt

Proinsulin has three distinct regions: the well-folded A- and B-chains and the dynamic disordered C-peptide. The highly conserved B-chain is a hotspot for diabetes-associated mutations, including the severe loss-of-function R(B22)Q mutation linked to childhood-onset diabetes. Here, we explore R(B22)'s role in proinsulin stability using AlphaFold-predicted structures and metadynamics simulations to achieve...

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Identifiers

PMID: 40305339
DOI: 10.3390/biom15040577
PMCID: PMC12025217

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