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

SASDF77 – Kinase-inducible domain interacting (KIX) domain of CREB-binding protein tethered to 1-10

Kinase-inducible domain interacting (KIX) domain of CREB-binding protein (CBP), mutation L664C
1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one

MW^experimental	11	kDa
MW^expected	11	kDa

log I(s) 2.96×10³ 2.96×10² 2.96×10¹ 2.96×10⁰

Kinase-inducible domain interacting (KIX) domain of CREB-binding protein (CBP), mutation L664C 1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 2.97×10³ R_g: 1.7 nm 0 (1.7 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 1.8 nm 0 D_max: 6.4 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.2

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.332
1.215

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of Kinase-inducible domain interacting (KIX) domain of CREB-binding protein tethered to 1-10 in 25 mM Hepes, 150 NaCl, 5% Glycerol, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; 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 3.88 mg/ml was measured at 10.2°C. 30 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.

Kinase-inducible domain interacting (KIX) domain of CREB-binding protein (CBP), mutation L664C (CBP KIX domain)
Mol. type		Protein
Organism		Mus musculus
Olig. state		Monomer
Mon. MW		10.5 kDa

UniProt		P45481 (586-672)
Sequence		FASTA

1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one (small molecule 1-10)
Mol. type		Other
Olig. state		Monomer
Mon. MW		0.4 kDa
Chemical formula