4JGW
The conformation of a docking site for SH3 domains is pre-selected in the Guanine Nucleotide Exchange Factor Rlf
Summary for 4JGW
| Entry DOI | 10.2210/pdb4jgw/pdb |
| Descriptor | Ral guanine nucleotide dissociation stimulator-like 2 (2 entities in total) |
| Functional Keywords | rem-domain, cdc25-homology domain, guanine nucleotide exchange factor, small g-protein binding, sh3 domain binding, signaling protein |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 104227.80 |
| Authors | Rehmann, H.,Popovic, M.,Jakobi, A.J. (deposition date: 2013-03-04, release date: 2013-09-11, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 23891840DOI: 10.1016/j.jsb.2013.07.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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