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Structure of bhpBR3, the BAFF-binding loop of BR3 embedded in a beta-hairpin peptide

Overview

The TNF-like ligand BAFF/BLyS is a potent survival factor for B cells. It, binds three receptors: TACI, BCMA, and BR3. We show that BR3 signaling, promotes processing of the transcription factor NF-kappaB2/p100 to p52., NF-kappaB2/p100 cleavage was abrogated in B cells from A/WySnJ mice, possessing a mutant BR3 gene, but not in TACI or BCMA null B cells., Furthermore, wild-type mice injected with BAFF-neutralizing BR3-Fc protein, showed reduced basal NF-kappaB2 activation. BR3-Fc treatment of NZB/WF1, mice, which develop a fatal lupus-like syndrome, inhibited NF-kappaB2, processing and attenuated the disease process. Since inhibiting the, BR3-BAFF interaction has therapeutic ramifications, the ligand binding, interface of BR3 was investigated and found to reside within a 26 residue, core domain. When stabilized within a structured beta-hairpin peptide, six, of these residues were sufficient to confer binding to BAFF.

About this Structure

1MPV is a Single protein structure of sequence from [1] with ACE and NH2 as ligands. Full crystallographic information is available from OCA.

Reference

BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-kappaB2., Kayagaki N, Yan M, Seshasayee D, Wang H, Lee W, French DM, Grewal IS, Cochran AG, Gordon NC, Yin J, Starovasnik MA, Dixit VM, Immunity. 2002 Oct;17(4):515-24. PMID:12387744

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