Structural highlights
Function
S10A1_HUMAN Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites.
Publication Abstract from PubMed
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 A 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.
X-ray crystal structure of human calcium-bound S100A1.,Melville Z, Aligholizadeh E, McKnight LE, Weber DJ, Pozharski E, Weber DJ Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):215-221. doi:, 10.1107/S2053230X17003983. Epub 2017 Mar 22. PMID:28368280[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Melville Z, Aligholizadeh E, McKnight LE, Weber DJ, Pozharski E, Weber DJ. X-ray crystal structure of human calcium-bound S100A1. Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):215-221. doi:, 10.1107/S2053230X17003983. Epub 2017 Mar 22. PMID:28368280 doi:http://dx.doi.org/10.1107/S2053230X17003983
