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X-ray crystal structure of human calcium-bound S100A1.

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.

SUBMITTER: Melville Z

PROVIDER: S-EPMC5379171 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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X-ray crystal structure of human calcium-bound S100A1.

Melville Zephan Z Aligholizadeh Ehson E McKnight Laura E LE Weber Dylan J DJ Pozharski Edwin E Weber David J DJ

Acta crystallographica. Section F, Structural biology communications 20170322 Pt 4

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 ...[more]

PMID: 28368280

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