RGL的Ras结合结构域的溶液结构

Solution structure of the Ras-binding domain of RGL.

作者信息

Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S

机构信息

Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama, Japan.

出版信息

FEBS Lett. 1998 Dec 28;441(3):413-8. doi: 10.1016/s0014-5793(98)01596-8.

DOI:10.1016/s0014-5793(98)01596-8

PMID:9891982

Abstract

The RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded beta-sheet and two alpha-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD.

摘要

RGL蛋白是Ral GDP解离刺激因子（RalGDS）的同源物，已被确定为Ras的下游效应器。在本研究中，通过核磁共振光谱法确定了RGL的Ras结合结构域（RGL-RBD）的溶液结构。RGL-RBD的整体折叠由一个五链β-折叠和两个α-螺旋组成，这与RalGDS-RBD的拓扑结构相同。还研究了RGL-RBD与结合GTP类似物的Ras相互作用时的主链化学位移扰动。RGL-RBD的溶液结构，特别是在一些与Ras相互作用的残基周围，与RalGDS-RBD明显不同。