Premium
X‐ray crystal structure of human calcium‐bound S100A1
Author(s) -
Melville Zephan,
Aligholizadeh Ehson,
McKnight Laura E.,
Weber Dylan J.,
Pozharski Edwin,
Weber David J.
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17003983
Subject(s) - s100 protein , calcium binding protein , chemistry , function (biology) , calcium , microbiology and biotechnology , biology , computational biology , immunology , immunohistochemistry , organic chemistry
S100A1 is a member of the S100 family of Ca 2+ ‐binding proteins and regulates several cellular processes, including those involved in Ca 2+ 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 Ca 2+ ‐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.