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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Experimental support for a β-propeller domain in integrin α -subunits and a calcium binding site on its lower surface
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Experimental support for a β-propeller domain in integrin α -subunits and a calcium binding site on its lower surface

机译:整合素α-亚基中的β-螺旋结构域及其下表面钙结合位点的实验支持

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摘要

Integrins are large, heterodimeric surface molecules of wide importance in cell adhesion. The N-terminal half of all integrin α-subunits contains seven weak sequence repeats of ≈60 amino acids that are important in ligand binding and have been predicted to fold cooperatively into a single β-propeller domain with seven β-sheets. We provide evidence supporting this model with a mouse mAb to human Mac-1 (αMβ2, CD11b/CD18). This antibody, CBRM1/20, binds to amino acid residues that are in different repeats and are 94 residues apart in the primary structure in the loop between strands 1 and 2 of β-sheet 5 and in the loop between strands 3 and 4 of β-sheet 6.
机译:整联蛋白是在细胞粘附中具有重要意义的大的异二聚体表面分子。所有整联蛋白α亚基的N末端一半包含七个≈60个氨基酸的弱序列重复序列,这些重复序列在配体结合中很重要,并且据预测可以协同折叠成具有七个β-折叠的单个β-螺旋结构域。我们提供了针对人类Mac-1的小鼠单克隆抗体(αMβ2,CD11b / CD18)支持该模型的证据。该抗体CBRM1 / 20与不同重复序列上的氨基酸残基结合,在β-折叠5的链1和2之间的环中以及在β的链3和4之间的环中的一级结构中相距94个残基页6。

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