The guanine nucleotide exchange factor Rlf interacts with SH3 domain-containing proteins via a binding site with a preselected conformation.

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.

journal_name

J Struct Biol

authors

Popovic M,Jakobi AJ,Rensen-de Leeuw M,Rehmann H

doi

10.1016/j.jsb.2013.07.009

subject

Has Abstract

pub_date

2013-09-01 00:00:00

pages

312-319

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(13)00189-5

journal_volume

183

pub_type

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