Visualizing a new binding site of ncd-motor domain on tubulin

被引：7

作者：

Han, Y

Sablin, EP

Nogales, E

Fletterick, RJ

Downing, KH ^{[1
]}

机构：

[1] Univ Calif Berkeley, Lawrence Berkeley Lab, Donner Lab, Div Life Sci, Berkeley, CA 94720 USA

[2] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA

[3] Univ Calif Berkeley, Dept Mol & Cellular Biol, Berkeley, CA 94720 USA

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 1999年 / 128卷 / 01期

关键词：

D O I：

10.1006/jsbi.1999.4162

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ncd is a microtubule minus-end directed motor of the kinesin superfamily. Previously it has been shown that ncd and kinesin motor domains share the same major binding site on microtubules. sere we report a three-dimensional EM reconstruction of negatively stained two-dimensional Zn-induced tubulin crystal sheets (Zn-sheets) decorated with the ncd motor domain at a resolution of 16 Angstrom This work has revealed a second specific binding site for the ncd motor domain. The motor binding site on the tubulin Zn-sheets spans both alpha and beta tubulin subunits. This binding site is located at a position different from the previously identified ncd binding site on microtubules and may play a role in motor function. (C) 1999 Academic Press.

引用

页码：26 / 33

页数：8

共 31 条

[11] Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry [J].