Title : Mechanism of Zn2+ and Ca2+ Binding to Human S100A1.

Pub. Date : 2021 Dec 3

PMID : 34944467






5 Functional Relationships(s)
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1 Using competitive binding experiments between Ca2+ and Zn2+ and QM/MM molecular modeling we conclude that Zn2+ high affinity sites are located in the EF-hand motifs of S100A1. Zinc carbonic anhydrase 2 Homo sapiens
2 Using competitive binding experiments between Ca2+ and Zn2+ and QM/MM molecular modeling we conclude that Zn2+ high affinity sites are located in the EF-hand motifs of S100A1. Zinc carbonic anhydrase 2 Homo sapiens
3 In addition, two lower affinity sites can bind Zn2+ even when the EF-hands are saturated by Ca2+, resulting in a 2Ca2+:S100A1:2Zn2+ conformer. Zinc carbonic anhydrase 2 Homo sapiens
4 We also determined a higher affinity to Ca2+ (KD~0.16 and 24 mum) than was previously reported for S100A1, which would allow this protein to function as a Ca2+/Zn2+-sensor both inside and outside cells, participating in diverse signaling pathways under normal and pathological conditions. Zinc carbonic anhydrase 2 Homo sapiens
5 We also determined a higher affinity to Ca2+ (KD~0.16 and 24 mum) than was previously reported for S100A1, which would allow this protein to function as a Ca2+/Zn2+-sensor both inside and outside cells, participating in diverse signaling pathways under normal and pathological conditions. Zinc carbonic anhydrase 2 Homo sapiens