Structural and biophysical analysis of the four CHRD domains of human chordin reveals a novel binding site for glycosaminoglycans.

Snee M, Birchenough HL, Becker MH Popplewell JF, Ashe HL, Baldock C, J Biol Chem :113248 (2026) Europe PMC

SASDY96 – Chordin fragment aa.168-650

Chordin fragment aa.168-650
MWexperimental 61 kDa
MWexpected 54 kDa
VPorod 106 nm3
log I(s) 1.15×10-1 1.15×10-2 1.15×10-3 1.15×10-4
Chordin fragment aa.168-650 small angle scattering data  s, nm-1
ln I(s)
Chordin fragment aa.168-650 Guinier plot ln 1.16×10-1 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Chordin fragment aa.168-650 Kratky plot 1.104 0 √3 sRg
p(r)
Chordin fragment aa.168-650 pair distance distribution function Rg: 3.0 nm 0 Dmax: 10.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Chordin fragment aa.168-650 MULTIFOXS model
Chordin fragment aa.168-650 MULTIFOXS model
log I(s)
 s, nm-1
Chordin fragment aa.168-650 MULTIFOXS model
Synchrotron SAXS data from solutions of Chordin fragment aa.168-650 in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 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 50.00 μl sample at 9 mg/ml was injected at a 0.07 ml/min flow rate onto a Cytiva Superdex 200 Increase 3.2/300 column at 15°C. 600 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.

Chordin fragment aa.168-650
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   53.6 kDa
 
UniProt   Q9H2X0-1 (168-644)
Sequence   FASTA