1ODB
THE CRYSTAL STRUCTURE OF HUMAN S100A12 - COPPER COMPLEX
Summary for 1ODB
| Entry DOI | 10.2210/pdb1odb/pdb |
| Related | 1E8A 1GQM |
| Descriptor | CALGRANULIN C, COPPER (II) ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | metal-binding protein, calcium-binding protein, s100 protein, ef-hand, calcium binding, host-parasite response, metal binding protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 6 |
| Total formula weight | 65621.48 |
| Authors | Moroz, O.V.,Antson, A.A.,Grist, S.J.,Maitland, N.J.,Dodson, G.G.,Wilson, K.S.,Lukanidin, E.M.,Bronstein, I.B. (deposition date: 2003-02-15, release date: 2003-06-12, Last modification date: 2023-12-13) |
| Primary citation | Moroz, O.V.,Antson, A.A.,Grist, S.J.,Maitland, N.J.,Dodson, G.G.,Wilson, K.S.,Lukanidin, E.M.,Bronstein, I.B. Structure of the Human S100A12-Copper Complex: Implications for Host-Parasite Defence Acta Crystallogr.,Sect.D, 59:859-, 2003 Cited by PubMed Abstract: S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins. Together with S100A8 and S100A9, it belongs to the calgranulin subfamily, i.e. it is mainly expressed in granulocytes, although there is an increasing body of evidence of expression in keratinocytes and psoriatic lesions. As well as being linked to inflammation, allergy and neuritogenesis, S100A12 is involved in host-parasite response, as are the other two calgranulins. Recent data suggest that the function of the S100-family proteins is modulated not only by calcium, but also by other metals such as zinc and copper. Previously, the structure of human S100A12 in low-calcium and high-calcium structural forms, crystallized in space groups R3 and P2(1), respectively, has been reported. Here, the structure of S100A12 in complex with copper (space group P2(1)2(1)2; unit-cell parameters a = 70.6, b = 119.0, c = 90.2 A) refined at 2.19 A resolution is reported. Comparison of anomalous difference electron-density maps calculated with data collected with radiation of wavelengths 1.37 and 1.65 A shows that each monomer binds a single copper ion. The copper binds at an equivalent site to that at which another S100 protein, S100A7, binds zinc. The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response. PubMed: 12777802DOI: 10.1107/S0907444903004700 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
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