1ODB

THE CRYSTAL STRUCTURE OF HUMAN S100A12 - COPPER COMPLEX

1ODB の概要

• エントリーDOI: 10.2210/pdb1odb/pdb
• 関連するPDBエントリー: 1E8A 1GQM
• 分子名称: CALGRANULIN C, COPPER (II) ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: metal-binding protein, calcium-binding protein, s100 protein, ef-hand, calcium binding, host-parasite response, metal binding protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 65621.48

構造登録者

Moroz, O.V.,Antson, A.A.,Grist, S.J.,Maitland, N.J.,Dodson, G.G.,Wilson, K.S.,Lukanidin, E.M.,Bronstein, I.B. (登録日: 2003-02-15, 公開日: 2003-06-12, 最終更新日: 2023-12-13)

主引用文献

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

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: 12777802
DOI: 10.1107/S0907444903004700

実験手法

X-RAY DIFFRACTION (2.19 Å)