1MPV

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

1MPV の概要

• エントリーDOI: 10.2210/pdb1mpv/pdb
• 分子名称: BLyS Receptor 3 (1 entity in total)
• 機能のキーワード: beta-hairpin, protein binding
• 細胞内の位置: Membrane; Single-pass type III membrane protein (Probable): Q96RJ3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1593.92

構造登録者

Kayagaki, N.,Yan, M.,Seshasayee, D.,Wang, H.,Lee, W.,French, D.M.,Grewal, I.S.,Cochran, A.G.,Gordon, N.C.,Yin, J.,Starovasnik, M.A.,Dixit, V.M. (登録日: 2002-09-12, 公開日: 2002-10-30, 最終更新日: 2024-10-30)

主引用文献

Kayagaki, N.,Yan, M.,Seshasayee, D.,Wang, H.,Lee, W.,French, D.M.,Grewal, I.S.,Cochran, A.G.,Gordon, N.C.,Yin, J.,Starovasnik, M.A.,Dixit, V.M.
BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-kappaB2.
Immunity, 17:515-524, 2002

PubMed Abstract: 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.

PubMed: 12387744
DOI: 10.1016/S1074-7613(02)00425-9

実験手法

SOLUTION NMR