PDBsum entry 5drv

Protein binding

PDB id: 5drv

Contents

Protein chain

131 a.a.

Ligands

LEU-THR-PHE-GLY-ASP-PHE-ASP-GLU

PDB id:

5drv

Name:

Protein binding

Title:

Crystal structure of the g3bp2 ntf2-like domain in complex with a peptide

Structure:

Ras gtpase-activating protein-binding protein 2. Chain: a. Fragment: ntf2-like domain, unp residues 1-139. Synonym: g3bp-2,gap sh3 domain-binding protein 2. Engineered: yes. Non-structural protein 3. Chain: b. Fragment: unp residues 1785-1792. Synonym: nsp3.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: g3bp2, kiaa0660. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Semliki forest virus. Sfv.

Resolution:

2.75Å R-factor: 0.250 R-free: 0.299

Authors:

O.Kristensen

Key ref:

O.Kristensen (2015). Crystal structure of the G3BP2 NTF2-like domain in complex with a canonical FGDF motif peptide. Biochem Biophys Res Commun, 467, 53-57. PubMed id: 26410532 DOI: 10.1016/j.bbrc.2015.09.123

Date:

16-Sep-15 Release date: 14-Oct-15

Protein chain

Q9UN86  (G3BP2_HUMAN) -  Ras GTPase-activating protein-binding protein 2 from Homo sapiens

Seq: 482 a.a.

Struc: 131 a.a.

DOI no: 10.1016/j.bbrc.2015.09.123

Biochem Biophys Res Commun 467:53-57 (2015)

PubMed id: 26410532

Crystal structure of the G3BP2 NTF2-like domain in complex with a canonical FGDF motif peptide.

O.Kristensen.

ABSTRACT

The crystal structure of the NTF2-like domain of the human Ras GTPase SH3 Binding Protein (G3BP), isoform 2, was determined at a resolution of 2.75 Å in complex with a peptide containing a FGDF sequence motif. The overall structure of the protein is highly similar to the homodimeric N-terminal domains of the G3BP1 and Rasputin proteins. Recently, a subset of G3BP interacting proteins was recognized to share a common sequence motif, FGDF. The most studied binding partners, USP10 and viral nsP3, interfere with essential G3BP functions related to assembly of cellular stress granules. Reported molecular modeling suggested that FGDF-motif containing peptides bind in an extended conformation into a hydrophobic groove on the surface of the G3BP NTF2-like domain in a manner similar to the known binding of FxFG nucleoporin repeats. The results in this paper provide evidence for a different binding mode. The FGDF peptide binds and changes conformation of the protruding N-terminal residues by providing hydrophobic interactions to a symmetry related molecule that facilitated crystallization of the G3BP2 isoform.