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 Bioljournal_title
Journal of structural biologyauthors
Popovic M,Jakobi AJ,Rensen-de Leeuw M,Rehmann Hdoi
10.1016/j.jsb.2013.07.009subject
Has Abstractpub_date
2013-09-01 00:00:00pages
312-319issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(13)00189-5journal_volume
183pub_type
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