| Literature DB >> 28368280 |
Zephan Melville1, Ehson Aligholizadeh1, Laura E McKnight1, Dylan J Weber1, Edwin Pozharski1, David J Weber1.
Abstract
S100A1 is a member of the S100 family of Ca2+-binding proteins and regulates several cellular processes, including those involved in Ca2+ signaling and cardiac and skeletal muscle function. In Alzheimer's disease, brain S100A1 is overexpressed and gives rise to disease pathologies, making it a potential therapeutic target. The 2.25 Å resolution crystal structure of Ca2+-S100A1 is solved here and is compared with the structures of other S100 proteins, most notably S100B, which is a highly homologous S100-family member that is implicated in the progression of malignant melanoma. The observed structural differences in S100A1 versus S100B provide insights regarding target protein-binding specificity and for targeting these two S100 proteins in human diseases using structure-based drug-design approaches.Entities:
Keywords: Alzheimer's disease; S100; S100A1; S100B; calcium-binding proteins; cardiomyopathy; crystal structure
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Year: 2017 PMID: 28368280 PMCID: PMC5379171 DOI: 10.1107/S2053230X17003983
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056