PDBsum entry 4wnd

Signaling protein/protein binding

PDB id: 4wnd

Contents

Protein chains

329 a.a.

26 a.a.

Ligands

SCN ×7

PEG ×5

PGE

EDO ×6

Waters ×298

PDB id:

4wnd

Name:

Signaling protein/protein binding

Title:

Crystal structure of the tpr domain of lgn in complex with frmpd4/preso1 at 1.5 angstrom resolution

Structure:

G-protein-signaling modulator 2. Chain: a. Fragment: n-terminal tpr domain, unp residues 20-421. Synonym: mosaic protein lgn. Engineered: yes. Ferm and pdz domain-containing protein 4. Chain: b. Fragment: frmpd4-l, unp residues 978-1025. Synonym: pdz domain-containing protein 10,psd-95-interacting

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: gpsm2, lgn. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: frmpd4, kiaa0316, pdzd10, pdzk10.

Resolution:

1.50Å R-factor: 0.164 R-free: 0.182

Authors:

H.Takayanagi,S.Yuzawa,H.Sumimoto

Key ref:

H.Takayanagi et al. (2015). Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN. Acta Crystallogr F Struct Biol Commun, 71, 175-183. PubMed id: 25664792 DOI: 10.1107/S2053230X14028143

Date:

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

Protein chain

P81274  (GPSM2_HUMAN) -  G-protein-signaling modulator 2 from Homo sapiens

Seq: 684 a.a.

Struc: 329 a.a.

Protein chain

Q14CM0  (FRPD4_HUMAN) -  FERM and PDZ domain-containing protein 4 from Homo sapiens

Seq: 1322 a.a.

Struc: 26 a.a.

DOI no: 10.1107/S2053230X14028143

Acta Crystallogr F Struct Biol Commun 71:175-183 (2015)

PubMed id: 25664792

Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN.

H.Takayanagi, S.Yuzawa, H.Sumimoto.

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.