5CM8

Structural Basis for the Selectivity of Guanine Nucleotide Exchange Factors for the small G-protein Ral

5CM8 の概要

• エントリーDOI: 10.2210/pdb5cm8/pdb
• 関連するPDBエントリー: 5CM9
• 分子名称: Ral guanine nucleotide dissociation stimulator-like 2, Ras-related protein Ral-a (3 entities in total)
• 機能のキーワード: complex g-protein exchange factor, signaling protein
• 由来する生物種: Mus musculus (House Mouse); 詳細
• 細胞内の位置: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P48555
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75231.18

構造登録者

Popovic, M.,Schouten, A.,Rehmann, H. (登録日: 2015-07-16, 公開日: 2016-01-13, 最終更新日: 2024-01-10)

主引用文献

Popovic, M.,Schouten, A.,Rensen-de Leeuw, M.,Rehmann, H.
The structure of the Guanine Nucleotide Exchange Factor Rlf in complex with the small G-protein Ral identifies conformational intermediates of the exchange reaction and the basis for the selectivity.
J.Struct.Biol., 193:106-114, 2016

PubMed Abstract: CDC25 homology domain (CDC25-HD) containing Guanine Nucleotide Exchange Factors (GEFs) initiate signalling by small G-proteins of the Ras-family. Each GEF acts on a small subset of the G-proteins only, thus providing signalling selectivity. Rlf is a GEF with selectivity for the G-proteins RalA and RalB. Here the crystal structure of Rlf in complex with Ral is determined. The Rlf·Ral complex crystallised into two different crystal forms, which represent different steps of the exchange reaction. Thereby general insight in the CDC25-HD catalysed nucleotide exchange is obtained. In addition, the basis for the selectivity of the interaction is investigated. The exchange activity is monitored by the use of recombinant proteins. Selectivity determinants in the binding interface are identified and confirmed by a mutational study.

PubMed: 26687416
DOI: 10.1016/j.jsb.2015.12.006

実験手法

X-RAY DIFFRACTION (2.6 Å)