CRYSTAL-STRUCTURE OF THE EXTRACELLULAR REGION OF HUMAN TISSUE FACTOR
CRYSTAL-STRUCTURE OF THE EXTRACELLULAR REGION OF HUMAN TISSUE FACTOR
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DOI：
10.1038/370662a0
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发表时间：
1994-08-25
期刊：
影响因子：
64.8
通讯作者：
BOYS, CWG
中科院分区：
文献类型：
--
作者：
HARLOS, K;MARTIN, DMA;BOYS, CWG
TISSUE 因子是一种细胞表面糖蛋白受体，在血管损伤后通过与凝血因子 VII/VIIa 相互作用启动凝血级联，并参与多种病理过程 (1)。当与组织因子结合时，因子 VII 很容易通过痕量的因子 Xa、IXa 或 VIIa 转化为活性蛋白酶因子 VIIa。人组织因子由 263 个残基组成，其中前 219 个残基构成细胞外区域(2)。我们以 2.2 埃的分辨率确定了细胞外区域的晶体结构。组织因子由两个通过广泛的、新颖的域间界面区域关联的免疫球蛋白样结构域组成。因子 VII 的结合位点位于界面区域，涉及结构域 1 的残基和结构域 2 的延伸环（结合“指”）。这是第 2 类细胞因子受体家族代表的结构，该家族还包括干扰素 α、干扰素 γ（参考文献 2、3）和白细胞介素 10（参考文献 4）受体。
TISSUE factor is a cell-surface glycoprotein receptor which initiates the blood coagulation cascade after vessel injury by interacting with blood clotting factor VII/VIIa and which is implicated in various pathological processes(1). When bound to tissue factor, factor VII is readily converted to the active protease factor VIIa by trace amounts of factors Xa, IXa or VIIa. Human tissue factor consists of 263 residues, the first 219 of which comprise the extracellular region(2). We have determined the crystal structure of the extracellular region at a resolution of 2.2 Angstrom. Tissue factor consists of two immunoglobulin-like domains associated through an extensive, novel, interdomain interface region. The binding site for factor VII lies at the interface region and involves residues from domain 1 and an extended loop (binding 'finger') of domain 2. This is the first reported structure of a representative of the class 2 cytokine receptor family, which also includes interferon-alpha, interferon-gamma (refs 2, 3) and interleukin-10 (ref. 4) receptors.