Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein.

Garg A, Orru R, Ye W, Distler U, Chojnacki JE, Köhn M, Tenzer S, Sönnichsen C, Wolf E, J Biol Chem (2019) Europe PMC

SASDF27 – Brain and Muscle ARNT-Like 1 from Mus musculus (D530-L625), monomer, trans-conformation locking mutation P624A

Aryl hydrocarbon receptor nuclear translocator-like protein 1
MWexperimental 13 kDa
MWexpected 10 kDa
log I(s) 2.55×103 2.55×102 2.55×101 2.55×100
Aryl hydrocarbon receptor nuclear translocator-like protein 1 small angle scattering data  s, nm-1
ln I(s)
Aryl hydrocarbon receptor nuclear translocator-like protein 1 Guinier plot ln 2.55×103 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Aryl hydrocarbon receptor nuclear translocator-like protein 1 Kratky plot 1.104 0 3 sRg
p(r)
Aryl hydrocarbon receptor nuclear translocator-like protein 1 pair distance distribution function Rg: 3.0 nm 0 Dmax: 11 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Aryl hydrocarbon receptor nuclear translocator-like protein 1 DAMMIN model

Synchrotron SAXS data from solutions of Brain and Muscle ARNT-Like 1 from Mus musculus (D530-L625), monomer, trans-conformation locking mutation P624A in 25 mM Hepes, 150 NaCl, 1 mM DTT, 5% Glycerol, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.27 mg/ml was measured at 10.1°C. 28 successive 0.045 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.

Aryl hydrocarbon receptor nuclear translocator-like protein 1 (BMAL1 P624A)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   9.9 kDa
 
UniProt   Q9WTL8-2 (530-625)
Sequence   FASTA