PDBsum entry 4g2v

Protein binding

PDB id: 4g2v

Contents

Protein chains

321 a.a.

17 a.a.

Ligands

GOL ×8

BTB

Metals

_CL

Waters ×84

PDB id:

4g2v

Name:

Protein binding

Title:

Structure complex of lgn binding with frmpd1

Structure:

G-protein-signaling modulator 2. Chain: a. Fragment: tpr domain, unp residues 22-357. Synonym: pins homolog. Engineered: yes. Peptide from ferm and pdz domain-containing protein 1. Chain: b. Fragment: unp residues 901-938. Synonym: ferm domain-containing protein 2.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

Resolution:

2.40Å R-factor: 0.192 R-free: 0.232

Authors:

Y.Shang,Z.Pan,W.Wen,W.Wang,M.Zhang

Key ref:

Z.Pan et al. (2013). Structural and biochemical characterization of the interaction between LGN and Frmpd1. J Mol Biol, 425, 1039-1049. PubMed id: 23318951 DOI: 10.1016/j.jmb.2013.01.003

Date:

13-Jul-12 Release date: 23-Jan-13

Protein chain

Q8VDU0  (GPSM2_MOUSE) -  G-protein-signaling modulator 2 from Mus musculus

Seq: 679 a.a.

Struc: 321 a.a.*

Protein chain

Q5SYB0  (FRPD1_HUMAN) -  FERM and PDZ domain-containing protein 1 from Homo sapiens

Seq: 1578 a.a.

Struc: 17 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1016/j.jmb.2013.01.003

J Mol Biol 425:1039-1049 (2013)

PubMed id: 23318951

Structural and biochemical characterization of the interaction between LGN and Frmpd1.

Z.Pan, Y.Shang, M.Jia, L.Zhang, C.Xia, M.Zhang, W.Wang, W.Wen.

ABSTRACT

The tetratricopeptide repeat (TPR) motif-containing protein LGN binds multiple targets and regulates their subcellular localizations and functions during both asymmetric and symmetric cell divisions. Here, we characterized the interaction between LGN-TPR motifs and FERM and PDZ domain containing 1 (Frmpd1) and reported the crystal structure of the complex at 2.4Å resolution. A highly conserved fragment at the center of Frmpd1 of ~20 residues was found to be necessary and sufficient to bind to LGN-TPR. This Frmpd1 fragment forms an extended structure and runs along the concave channel of the TPR superhelix in an antiparallel manner in the complex. Structural comparisons and biochemical studies of LGN/Frmpd1 and other known LGN/target interactions demonstrate that the LGN-TPR motifs are versatile and capable of recognizing multiple targets via diverse binding modes. Nevertheless, a conserved "E/QxEx4-5E/D/Qx1-2K/R" motif in LGN/Pins (partner of inscuteable) TPR binding proteins has been identified.