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可交换GTP结合位点在微管正端的定位。

Localization of an exchangeable GTP binding site at the plus end of microtubules.

作者信息

Mitchison T J

机构信息

Department of Pharmacology, University of California, San Francisco 94143-0450.

出版信息

Science. 1993 Aug 20;261(5124):1044-7. doi: 10.1126/science.8102497.

Abstract

Microtubule polarity arises from the head-to-tail orientation of alpha-beta tubulin heterodimers in the microtubule lattice. The identity of the polypeptide at each end of the microtubule is unknown, but structural models predict that the beta-tubulin end contains an exchangeable guanosine triphosphate (GTP) binding site. When GTP-coated fluorescent beads were incubated with microtubules, they bound specifically to plus ends, suggesting that tubulin is oriented in microtubules with beta-tubulin toward the plus end.

摘要

微管极性源于微管晶格中α-β微管蛋白异二聚体的头对尾排列方向。微管两端多肽的特性尚不清楚,但结构模型预测β-微管蛋白端含有一个可交换的鸟苷三磷酸(GTP)结合位点。当用包被有GTP的荧光珠与微管一起温育时,它们特异性地结合到正端,这表明微管蛋白在微管中的排列是β-微管蛋白朝向正端。

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