1MPV: BLyS Receptor 3

Structure of bhpBR3, the BAFF-binding loop of BR3 embedded in a beta-hairpin peptide. Determined by solution NMR. Released 30 Oct 2002.

Method: Solution NMR
Chains: 1
Atoms: 113
Mol. weight: 1.59 kDa
Released: 30 Oct 2002

Explore 1MPV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MPV contains 0 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	24-26	3	1
β-strand	31-33	3	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
BLyS Receptor 3	A	protein	14		Q96RJ3 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MPV_1 BLyS Receptor 3 (chains A)
XCHWDLLVRHWVCX

Primary citation

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. et al. Immunity (2002) 17:515-524. DOI 10.1016/S1074-7613(02)00425-9 · PubMed

Other PDB entries of the same protein (UniProt Q96RJ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1OQE 2.5 Å, Crystal structure of sTALL-1 with BAFF-R
8ZUJ 2.58 Å, Pentagonal cluster of BAFF-BAFFR ectodomain complex
2HFG 2.61 Å, Crystal structure of hBR3 bound to CB3s-Fab
8ZUK 2.83 Å, Cluster structure of the BAFF-BAFFR-TRAF3 complex
3V56 3.0 Å, Re-refinement of PDB entry 1OSG - Complex between BAFF and a BR3 derived peptide…
4V46 3.3 Å, Crystal structure of the BAFF-BAFF-R complex
1OSX Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3)

Browse structure collections

About this viewer

MolViewer shows 1MPV directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.