4JGW

The conformation of a docking site for SH3 domains is pre-selected in the Guanine Nucleotide Exchange Factor Rlf

4JGW の概要

• エントリーDOI: 10.2210/pdb4jgw/pdb
• 分子名称: Ral guanine nucleotide dissociation stimulator-like 2 (2 entities in total)
• 機能のキーワード: rem-domain, cdc25-homology domain, guanine nucleotide exchange factor, small g-protein binding, sh3 domain binding, signaling protein
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104227.80

構造登録者

Rehmann, H.,Popovic, M.,Jakobi, A.J. (登録日: 2013-03-04, 公開日: 2013-09-11, 最終更新日: 2023-11-08)

主引用文献

Popovic, M.,Jakobi, A.J.,Rensen-de Leeuw, M.,Rehmann, H.
The guanine nucleotide exchange factor Rlf interacts with SH3 domain-containing proteins via a binding site with a preselected conformation.
J.Struct.Biol., 183:312-319, 2013

PubMed Abstract: Rlf is a guanine nucleotide exchange factor for the small G-proteins RalA and RalB and couples Ras- to Ral-signalling. Here the crystal structure of the catalytic module of Rlf consisting of a REM- and a CDC25-homology domain is determined. The structure is distinguished by an extended three stranded β-sheet called the flagpole. The flagpole is a conserved element in the RalGDS family of guanine nucleotide exchange factors and stabilises the orientation of the REM-domain relative to the CDC25-homology domain. A proline-rich sequence in the flagpole is unique to Rlf and several proteins that interact with this sequence by SH3 domains are identified. Conformational pre-selection results in a gain of affinity and contributes to the establishment of SH3 domain selectivity.

PubMed: 23891840
DOI: 10.1016/j.jsb.2013.07.009

実験手法

X-RAY DIFFRACTION (2.3 Å)