6FIE
Crystallographic structure of calcium loaded Calbindin-D28K.
Summary for 6FIE
| Entry DOI | 10.2210/pdb6fie/pdb |
| Related | 2G9B |
| Descriptor | Calbindin, CALCIUM ION, THIOCYANATE ION, ... (4 entities in total) |
| Functional Keywords | calcium binding protein, buffer, impase, ef-hand, metal binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 30570.78 |
| Authors | Noble, J.W.,Almalki, R.,Roe, S.M.,Wagner, A.,Dumanc, R.,Atack, J.R. (deposition date: 2018-01-18, release date: 2018-10-10, Last modification date: 2024-05-01) |
| Primary citation | Noble, J.W.,Almalki, R.,Roe, S.M.,Wagner, A.,Duman, R.,Atack, J.R. The X-ray structure of human calbindin-D28K: an improved model. Acta Crystallogr D Struct Biol, 74:1008-1014, 2018 Cited by PubMed Abstract: Calbindin-D28K is a widely expressed calcium-buffering cytoplasmic protein that is involved in many physiological processes. It has been shown to interact with other proteins, suggesting a role as a calcium sensor. Many of the targets of calbindin-D28K are of therapeutic interest: for example, inositol monophosphatase, the putative target of lithium therapy in bipolar disorder. Presented here is the first crystal structure of human calbindin-D28K. There are significant deviations in the tertiary structure when compared with the NMR structure of rat calbindin-D28K (PDB entry 2g9b), despite 98% sequence identity. Small-angle X-ray scattering (SAXS) indicates that the crystal structure better predicts the properties of calbindin-D28K in solution compared with the NMR structure. Here, the first direct visualization of the calcium-binding properties of calbindin-D28K is presented. Four of the six EF-hands that make up the secondary structure of the protein contain a calcium-binding site. Two distinct conformations of the N-terminal EF-hand calcium-binding site were identified using long-wavelength calcium single-wavelength anomalous dispersion (SAD). This flexible region has previously been recognized as a protein-protein interaction interface. SAXS data collected in both the presence and absence of calcium indicate that there are no large structural differences in the globular structure of calbindin-D28K between the calcium-loaded and unloaded proteins. PubMed: 30289411DOI: 10.1107/S2059798318011610 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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