Structural highlights
Publication Abstract from PubMed
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 beta-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.
The guanine nucleotide exchange factor Rlf interacts with SH3 domain-containing proteins via a binding site with a preselected conformation.,Popovic M, Jakobi AJ, Rensen-de Leeuw M, Rehmann H J Struct Biol. 2013 Sep;183(3):312-9. doi: 10.1016/j.jsb.2013.07.009. Epub 2013, Jul 24. PMID:23891840[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Popovic M, Jakobi AJ, 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. 2013 Sep;183(3):312-9. doi: 10.1016/j.jsb.2013.07.009. Epub 2013, Jul 24. PMID:23891840 doi:10.1016/j.jsb.2013.07.009
