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Article

Decoding Allostery: How Interactions Lock S100B Conformations and What K55A Mutation Teaches Us.

Journal of chemical information and modeling - 8 Dec 2025

Samanta Riya, Zhuang Xinhao, Gondolesi Manuel, Varney Kristen M, Weber David J, Matysiak Silvina

Abstract excerpt

Allostery, also called action at a distance and ubiquitous in biological systems, is so important that it is also hailed as "the second secret of life." In certain proteins, instead of conformational changes, proteins exhibit "dynamic" allostery. S100B is a Ca2+ binding protein, where TRTK binding enhances Ca2+ binding at a site 25 Å away from the metalation site and serves as a model to study "dynamic"...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 41267530
DOI: 10.1021/acs.jcim.5c02475
PMCID: PMC13389858

Genes

S100B

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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