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Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface.

Marcos R Calgaro¹, Mario de Oliveira Neto, Ana Carolina M Figueira

¹Instituto de Física de São Carlos, Departamento de Física e Informática, Universidade de São Paulo, CEP 13566-590 São Carlos, São Paulo, Brazil.

Protein Science : a Publication of the Protein Society

|June 30, 2007

Summary

The orphan receptor nerve growth factor-induced B (NGFI-B) forms a unique V-shaped dimer in solution, utilizing an unconventional interface distinct from other nuclear receptors. This structural insight is crucial for understanding NGFI-B

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Area of Science:

Molecular biology
Structural biology
Biochemistry

Background:

Nerve growth factor-induced B (NGFI-B) is an orphan nuclear receptor belonging to subfamily 4A (Nr4a).
NGFI-B exhibits unique DNA binding capabilities, acting as a monomer or homodimer on distinct DNA motifs.
Understanding the quaternary structure of NGFI-B is essential for elucidating its transcriptional regulation mechanisms.

Purpose of the Study:

To determine the solution structure of the NGFI-B ligand-binding domain (LBD).
To characterize the dimerization interface and structural organization of NGFI-B in solution.
To compare the dimerization mode of NGFI-B with other nuclear receptors.

Main Methods:

Small-angle X-ray scattering (SAXS) with ab initio modeling.
Hydrogen-deuterium exchange mass spectrometry (HDX-MS).

Main Results:

NGFI-B LBD forms dimers in solution with a radius of gyration of 2.9 nm and a maximum dimension of 9.0 nm.
The NGFI-B LBD dimer adopts a V-shaped conformation with a wider opening angle than estrogen receptor (ER) or retinoid X receptor (RXR).
Dimerization occurs through an extended surface area involving the loop between helices 3 and 4 and the C-terminal part of helix 3, differing from the classical nuclear receptor interface.

Conclusions:

NGFI-B forms a unique V-shaped dimer in solution through an unconventional interface.
The NGFI-B dimerization interface shares similarities with that of the glucocorticoid receptor (GR).
These findings provide insights into NGFI-B's DNA recognition and potential cross-talk with GR in transcriptional regulation.