1odb

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1odb, resolution 2.19Å

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THE CRYSTAL STRUCTURE OF HUMAN S100A12- COPPER COMPLEX

Overview

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.

About this Structure

1ODB is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of the human S100A12-copper complex: implications for host-parasite defence., Moroz OV, Antson AA, Grist SJ, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):859-67. Epub 2003, Apr 25. PMID:12777802

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