Structural Insights into the Unique Modes of Relaxin-Binding and Tethered-Agonist Mediated Activation of RXFP1 and RXFP2.

Sethi A, Bruell S, Ryan T, Yan F, Tanipour MH, Mok YF, Draper-Joyce C, Khandokar Y, Metcalfe RD, Griffin MDW, Scott DJ, Hossain MA, Petrie EJ, Bathgate RAD, Gooley PR, J Mol Biol 433(21):167217 (2021) Europe PMC

SASDLH7 – LDLa linker region of human Relaxin receptor 2 (RXFP2, 38-105)

Relaxin receptor 2
MWexperimental 6 kDa
MWexpected 7 kDa
VPorod 12 nm3
log I(s) 8.83×10-3 8.83×10-4 8.83×10-5 8.83×10-6
Relaxin receptor 2 small angle scattering data  s, nm-1
ln I(s)
Relaxin receptor 2 Guinier plot ln 8.83×10-3 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Relaxin receptor 2 Kratky plot 1.104 0 √3 sRg
Dmax: 7.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
LDLa linker region of human Relaxin receptor 2 (RXFP2, 38-105) Rg histogram Rg, nm
Relaxin receptor 2 EOM/RANCH model
Relaxin receptor 2 EOM/RANCH model
Relaxin receptor 2 EOM/RANCH model
Relaxin receptor 2 EOM/RANCH model
Synchrotron SAXS data from solutions of the LDLa linker region RXFP2 (38-105) in 20 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.1%NaN3, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.4 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 21.8°C. 20 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Relaxin receptor 2 (RXFP2(38-105))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   7.1 kDa
 
UniProt   Q8WXD0 (38-105)
Sequence   FASTA