5K89
Crystal Structure of Human Calcium-Bound S100A1
Summary for 5K89
| Entry DOI | 10.2210/pdb5k89/pdb |
| Descriptor | Protein S100-A1, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | s100, s100a1, calcium, metal binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 3 |
| Total formula weight | 32032.96 |
| Authors | Melville, Z.,Aligholizadeh, E.,McKnight, L.E.,Weber, D.,Pozharski, E.,Weber, D.J. (deposition date: 2016-05-27, release date: 2017-04-12, Last modification date: 2023-09-27) |
| Primary citation | Melville, Z.,Aligholizadeh, E.,McKnight, L.E.,Weber, D.J.,Pozharski, E.,Weber, D.J. X-ray crystal structure of human calcium-bound S100A1. Acta Crystallogr F Struct Biol Commun, 73:215-221, 2017 Cited by PubMed Abstract: S100A1 is a member of the S100 family of Ca-binding proteins and regulates several cellular processes, including those involved in Ca 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-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. PubMed: 28368280DOI: 10.1107/S2053230X17003983 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.249 Å) |
Structure validation
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