X-ray crystal structure of human calcium-bound S100A1
Copyright policy )X-ray crystal structure of human calcium-bound S100A1
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 S100A1versusS100B provide insights regarding target protein-binding specificity and for targeting these two S100 proteins in human diseases using structure-based drug-design approaches.
- University of Maryland, Baltimore United States
- University of Maryland Marlene and Stewart Greenebaum Cancer Center United States
- University of Maryland Medical System United States
Models, Molecular, Protein Conformation, alpha-Helical, Binding Sites, Cations, Divalent, Genetic Vectors, S100 Proteins, Gene Expression, S100 Calcium Binding Protein beta Subunit, Crystallography, X-Ray, Recombinant Proteins, Escherichia coli, Humans, Protein Isoforms, Calcium, Protein Interaction Domains and Motifs, Amino Acid Sequence, Cloning, Molecular, Protein Multimerization, Sequence Alignment, Protein Binding
Models, Molecular, Protein Conformation, alpha-Helical, Binding Sites, Cations, Divalent, Genetic Vectors, S100 Proteins, Gene Expression, S100 Calcium Binding Protein beta Subunit, Crystallography, X-Ray, Recombinant Proteins, Escherichia coli, Humans, Protein Isoforms, Calcium, Protein Interaction Domains and Motifs, Amino Acid Sequence, Cloning, Molecular, Protein Multimerization, Sequence Alignment, Protein Binding
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