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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of S100A12 in a hexameric form and its proposed role in receptor signalling.
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The structure of S100A12 in a hexameric form and its proposed role in receptor signalling.

机译：hexameric S100A12的形式和结构其拟议的作用受体信号。

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摘要

S100A12 is a member of the S100 subfamily of EF-hand calcium-binding proteins; it has been shown to be one of the ligands of the 'receptor for advanced glycation end products' (RAGE) that belongs to the immunoglobulin superfamily and is involved in diabetes, Alzheimer's disease, inflammation and tumour invasion. The structure of the dimeric form of native S100A12 from human granulocytes in the presence of calcium in space group R3 has previously been reported. Here, the structure of a second crystal form in space group P2(1) (unit-cell parameters a = 53.9, b = 100.5, c = 112.7A, beta = 94.6 degrees) solved at 2.7A resolution by molecular replacement using the R3 structure as a search model is reported. Like most S100 proteins, S100A12 is a dimer. However, in the P2(1) crystal form dimers of S100A12 are arranged in a spherical hexameric assembly with an external diameter of about 55 A stabilized by calcium ions bound between adjacent dimers. The putative target-binding sites of S100A12 are located at the outer surface of the hexamer, making it possible for the hexamer to bind several targets. It is proposed that the S100A12 hexameric assembly might interact with three extracellular domains of the receptor, bringing them together into large trimeric assemblies.
机译：S100A12属于S100的亚科类ef - hand钙结合蛋白质;是配体的受体之一高级糖化终端产品(愤怒)属于免疫球蛋白超家族,参与糖尿病、阿尔茨海默病炎症和肿瘤入侵。二聚的原生S100A12形式的人类粒细胞在钙的存在空间R3组曾被报道。第二个水晶形式在空间群的结构P2(1)(晶胞参数= 53.9,b = 100.5,c = 112.7,β= 94.6在2.7度)解决通过分子替换使用R3的决议报告结构作为搜索模型。大多数S100蛋白,S100A12二聚体。在P2(1)水晶S100A12二聚体的形式安排在一个球形hexameric组装外部直径约55的稳定钙离子结合相邻二聚体。假定的S100A12的约束性目标网站位于六聚体的外表面,使六聚物结合几个目标。hexameric组装可能会与三个细胞外的域受体,使在一起成大三聚物的程序集。

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