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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The active conformation of human glucokinase is not altered by allosteric activators.
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The active conformation of human glucokinase is not altered by allosteric activators.

机译：人类葡糖激酶的活性构象不改变变构活化剂。

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摘要

Glucokinase (GK) catalyses the formation of glucose 6-phosphate from glucose and ATP. A specific feature of GK amongst hexokinases is that it can cycle between active and inactive conformations as a function of glucose concentration, resulting in a unique positive kinetic cooperativity with glucose, which turns GK into a unique key sensor of glucose metabolism, notably in the pancreas. GK is a target of antidiabetic drugs aimed at the activation of GK activity, leading to insulin secretion. Here, the first structures of a GK-glucose complex without activator, of GK-glucose-AMP-PNP and of GK-glucose-AMP-PNP with a bound activator are reported. All these structures are extremely similar, thus demonstrating that binding of GK activators does not result in conformational changes of the active protein but in stabilization of the active form of GK.
机译：葡糖激酶(门将)催化作用的形成从葡萄糖和葡萄糖6-phosphate ATP。特定功能的门将在己糖激酶它可以循环之间的活跃的和不活跃的构象的葡萄糖浓度,导致一个独特的积极与葡萄糖动态协调,门将唯一键的葡萄糖传感器新陈代谢,尤其是在胰腺。抗糖尿病的药物针对的目标门将活动的激活,导致胰岛素分泌。GK-glucose没有激活,复杂的GK-glucose-AMP-PNP和GK-glucose-AMP-PNP一个绑定激活报道。结构极其相似,因此证明绑定的GK活化剂不会导致构象的变化积极稳定的蛋白质,但活跃形式的星期。

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