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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand.
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Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand.

机译：用聚糖楔稳定整联蛋白头部的开放构象，增加了对配体的亲和力。

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摘要

The affinity of the extracellular domain of integrins for ligand is regulated by conformational changes signaled from the cytoplasm. Alternative types of conformational movement in the ligand-binding headpiece have been proposed. In one study, electron micrograph image averages of the headpiece of integrin aVbeta3 show two different conformations. The open conformation of the headpiece is present when a ligand mimetic peptide is bound and differs from the closed conformation in the presence of an obtuse angle between the beta3 subunit hybrid and I-like domains. We tested the hypothesis that opening of the hybrid-I-like domain interface increases ligand-binding affinity by mutationally introducing an N-glycosylation site into it. Both beta3 and beta1 integrin glycan wedge mutants exhibit constitutively high affinity for physiological ligands. The data uniquely support one model of integrin activation and suggest that movement at the interface with the hybrid domain pulls down the C-terminal helix of theI-like domain and activates its metal ion-dependent adhesion site, analogously to activation of the integrin I domain.
机译：整联蛋白的细胞外结构域对配体的亲和力由细胞质发出的构象变化调节。已经提出了配体结合头部中的构象运动的其他类型。在一项研究中，整联蛋白aVbeta3头戴装置的电子显微图像平均值显示出两种不同的构象。当结合配体模拟肽时，头饰的开放构象存在，并且在beta3亚基杂合体和I样结构域之间存在钝角的情况下不同于封闭构象。我们测试了这样的假说，即通过将N-糖基化位点突变引入杂合I样结构域界面来增加配体结合亲和力。 beta3和beta1整合素聚糖楔形突变体都表现出对生理配体的组成性高亲和力。数据独特地支持整合素激活的一种模型，并表明与杂化域的界面处的运动会拉低I样域的C末端螺旋并激活其金属离子依赖性粘附位点，类似于整合素I域的激活。

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