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• W2912105446 abstract "This paper takes the cue from the previously solved crystal structure of human apo-S100Z and compares it with that of the calcium-bound S100Z from zebrafish in order to stress, for this particular S100, the significant role of the presence of calcium in promoting supramolecular assemblies with likely biological meaning. This consideration is then expanded through a wider review on analogous situations concerning all other S100s for which there is crystallographic o biochemical evidence of how the presence of calcium promotes the formation of quaternary complexes.The paper also deals with some considerations on the quality of the crystals obtained for the solved members of this family and on the need for experimental phasing for solving some of the structures where the good general sequence homology among the members of the family would have suggested molecular replacement (MR) as the easiest way to solve them.These considerations, along with the PCA analysis carried out on all the known S100s, further demonstrate that calcium plays a fundamental role in triggering quaternary structure formation for several members of this family of proteins." @default.
• W2912105446 created "2019-02-21" @default.
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• W2912105446 date "2019-01-01" @default.
• W2912105446 modified "2023-09-23" @default.
• W2912105446 title "Reviewing the Crystal Structure of S100Z and Other Members of the S100 Family: Implications in Calcium-Regulated Quaternary Structure" @default.
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• W2912105446 doi "https://doi.org/10.1007/978-1-4939-9030-6_30" @default.
• W2912105446 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30710292" @default.
• W2912105446 hasPublicationYear "2019" @default.
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