Structural basis for regulation of CELSR1 by a compact module in its extracellular region

Sumit Bandekar.

SASDVT7 – Cadherin EGF LAG seven-pass G-type receptor 1 (CELSR1) ECR with calcium

Cadherin EGF LAG seven-pass G-type receptor 1
MWexperimental 420 kDa
MWexpected 491 kDa
VPorod 722 nm3
log I(s) 2.18×100 2.18×10-1 2.18×10-2 2.18×10-3
Cadherin EGF LAG seven-pass G-type receptor 1 small angle scattering data  s, nm-1
ln I(s)
Cadherin EGF LAG seven-pass G-type receptor 1 Guinier plot ln 2.18×100 Rg: 16.2 nm 0 (16.2 nm)-2 s2
(sRg)2I(s)/I(0)
Cadherin EGF LAG seven-pass G-type receptor 1 Kratky plot 1.104 0 3 sRg
p(r)
Cadherin EGF LAG seven-pass G-type receptor 1 pair distance distribution function Rg: 16.7 nm 0 Dmax: 67.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of CELSR1 ECR with calcium in 10 mM Tris, 150 mM NaCl, 1 mM CaCl2, pH 8.5 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Eiger2 XE 9M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.1033 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 250.00 μl sample at 1.0 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superose 6 Increase 10/300 column at 22°C. 2500 successive 0.400 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.

Mismatched sheath (no CaCl2).

Cadherin EGF LAG seven-pass G-type receptor 1 (CELSR1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   245.4 kDa
 
UniProt   O35161 (255-2477)
Sequence   FASTA