Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism.

Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I, Nat Commun 16(1):3495 (2025) Europe PMC

SASDWV2 – Human immunoglobulin gamma 1 (IgG1) SAP1.3

Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain
Human immunoglobulin SAP1.3 - kappa chain
MWexperimental 147 kDa
MWexpected 147 kDa
VPorod 229 nm3
log I(s) 2.58×102 2.58×101 2.58×100 2.58×10-1
Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain Human immunoglobulin SAP1.3 - kappa chain small angle scattering data  s, nm-1
ln I(s)
Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain Human immunoglobulin SAP1.3 - kappa chain Guinier plot ln 2.58×102 Rg: 5.2 nm 0 (5.2 nm)-2 s2
(sRg)2I(s)/I(0)
Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain Human immunoglobulin SAP1.3 - kappa chain Kratky plot 1.104 0 3 sRg
p(r)
Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain Human immunoglobulin SAP1.3 - kappa chain pair distance distribution function Rg: 5.1 nm 0 Dmax: 16.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Human immunoglobulin gamma 1 (IgG1) SAP1.3 in 50 mM HEPES, 150 mM KCl, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 12.8 mg/ml was injected at a 0.25 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 20°C. 600 successive 2 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.

Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   49.7 kDa
Sequence   FASTA
 
Human immunoglobulin SAP1.3 - kappa chain
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   23.9 kDa
Sequence   FASTA