4WND

Crystal structure of the TPR domain of LGN in complex with Frmpd4/Preso1 at 1.5 Angstrom resolution

Summary for 4WND

• Entry DOI: 10.2210/pdb4wnd/pdb
• Related: 3SF4 4WNE 4WNF 4WNG
• Descriptor: G-protein-signaling modulator 2, FERM and PDZ domain-containing protein 4, THIOCYANATE ION, ... (7 entities in total)
• Functional Keywords: tetratricopeptide repeat, tpr, cell polarity, cytoplasm and cell cortex, signaling protein-protein binding complex, signaling protein/protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 52239.66

Authors

Takayanagi, H.,Yuzawa, S.,Sumimoto, H. (deposition date: 2014-10-11, release date: 2015-09-16, Last modification date: 2023-11-08)

Primary citation

Takayanagi, H.,Yuzawa, S.,Sumimoto, H.
Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN
Acta Crystallogr.,Sect.F, 71:175-183, 2015

PubMed Abstract: 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 Å 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 α-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.

PubMed: 25664792
DOI: 10.1107/S2053230X14028143

Experimental method

X-RAY DIFFRACTION (1.5 Å)