Structural Modeling and Dynamics of the Full-Length Homer1 Multimer.

Kálmán ZE, Czajlik A, Maruzs B, Farkas F, Pap I, Homonnay C, Klumpler T, Batta G, Gáspári Z, Péterfia B, Proteins (2025) Europe PMC

SASDXK2 – Enabled/vasodilator-stimulated phosphoprotein homology 1 domain (EVH1) from Mus musculus Homer1

EVH1 domain of Homer protein homolog 1 from mouse
MWexperimental 10 kDa
MWexpected 14 kDa
VPorod 23 nm3
log I(s) 3.18×10-1 3.18×10-2 3.18×10-3 3.18×10-4
EVH1 domain of Homer protein homolog 1 from mouse small angle scattering data  s, nm-1
ln I(s)
EVH1 domain of Homer protein homolog 1 from mouse Guinier plot ln 3.18×10-1 Rg: 1.6 nm 0 (1.6 nm)-2 s2
(sRg)2I(s)/I(0)
EVH1 domain of Homer protein homolog 1 from mouse Kratky plot 1.104 0 √3 sRg
p(r)
EVH1 domain of Homer protein homolog 1 from mouse pair distance distribution function Rg: 1.6 nm 0 Dmax: 5.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
EVH1 domain of Homer protein homolog 1 from mouse XPLOR-NIH model
SAXS data from solutions of Enabled/vasodilator-stimulated phosphoprotein homology 1 domain (EVH1) from Mus musculus Homer1 in 20mM NaCl, 50 mM NaPi, 0.02% of sodium-azide, pH 7.4 were collected on the Rigaku BioSAXS-2000 instrument (CEITEC, Brno, Czech Republic) using a Rigaku HyPix-3000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 25°C. Six successive 600 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.

EVH1 domain of Homer protein homolog 1 from mouse (EVH1 of Homer1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   13.7 kDa
 
UniProt   Q9Z2Y3 (1-118)
Sequence   FASTA