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PDBsum entry 4jgw

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protein Protein-protein interface(s) links
Signaling protein PDB id
4jgw

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
396 a.a.
Waters ×182
PDB id:
4jgw
Name: Signaling protein
Title: The conformation of a docking site for sh3 domains is pre-selected in the guanine nucleotide exchange factor rlf
Structure: Ral guanine nucleotide dissociation stimulator-like 2. Chain: a, b. Fragment: unp residues 50-514. Synonym: ralgds-like 2, ralgds-like factor, ras-associated protein rab2l. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: rgl2, rab2l, rlf. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.30Å     R-factor:   0.253     R-free:   0.288
Authors: H.Rehmann,M.Popovic,A.J.Jakobi
Key ref: M.Popovic et al. (2013). 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. PubMed id: 23891840 DOI: 10.1016/j.jsb.2013.07.009
Date:
04-Mar-13     Release date:   11-Sep-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q61193  (RGL2_MOUSE) -  Ral guanine nucleotide dissociation stimulator-like 2 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
778 a.a.
396 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1016/j.jsb.2013.07.009 J Struct Biol 183:312-319 (2013)
PubMed id: 23891840  
 
 
The guanine nucleotide exchange factor Rlf interacts with SH3 domain-containing proteins via a binding site with a preselected conformation.
M.Popovic, A.J.Jakobi, M.Rensen-de Leeuw, H.Rehmann.
 
  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.
 

 

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