4WNG: Crystal Structure Of The Tpr Domain Of Lgn In Complex With Frmpd4/preso1 At 2.1 Angstrom Resolution

The adaptor protein LGN interacts via the N-terminal domain comprising eight tetratricopeptide-repeat (TPR) motifs with its partner proteins mInsc, NuMA, Frmpd1 and Frmpd4 in a mutually exclusive manner. Here, the crystal structure of the LGN TPR domain in complex with human Frmpd4 is described at 1.5 A resolution. In the complex, the LGN-binding region of Frmpd4 (amino-acid residues 990-1011) adopts an extended structure that runs antiparallel to LGN along the concave surface of the superhelix formed by the TPR motifs. Comparison with the previously determined structures of the LGN-Frmpd1, LGN-mInsc and LGN-NuMA complexes reveals that these partner proteins interact with LGN TPR1-6 via a common core binding region with consensus sequence (E/Q)XEX4-5(E/D/Q)X1-2(K/R)X0-1(V/I). In contrast to Frmpd1, Frmpd4 makes additional contacts with LGN via regions N- and C-terminal to the core sequence. The N-terminal extension is replaced by a specific alpha-helix in mInsc, which drastically increases the direct contacts with LGN TPR7/8, consistent with the higher affinity of mInsc for LGN. A crystal structure of Frmpd4-bound LGN in an oxidized form is also reported, although oxidation does not appear to strongly affect the interaction with Frmpd4.
PDB ID: 4WNGDownload
MMDB ID: 132610
PDB Deposition Date: 2014/10/11
Updated in MMDB: 2015/09
Experimental Method:
x-ray diffraction
Resolution: 2.11  Å
Source Organism:
Similar Structures:
Biological Unit for 4WNG: dimeric; determined by author and by software (PISA)
Molecular Components in 4WNG
Label Count Molecule
Proteins (2 molecules)
G-protein-signaling Modulator 2(Gene symbol: GPSM2)
Molecule annotation
Ferm and PDZ Domain-containing Protein 4(Gene symbol: FRMPD4)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB