Modulation of Homer1 EVH1 domain internal dynamics by putative autism-associated mutations.

Farkas F, Maruzs B, Kálmán ZE, Klumpler T, Batta G, Péterfia B, Gáspári Z, FEBS Lett (2026) Europe PMC

SASDYW3 – Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer

Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer
MWexperimental 12 kDa
MWexpected 14 kDa
VPorod 24 nm3
log I(s) 7.22×10-1 7.22×10-2 7.22×10-3 7.22×10-4
Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer small angle scattering data  s, nm-1
ln I(s)
Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer Guinier plot ln 7.22×10-1 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer Kratky plot 1.104 0 √3 sRg
p(r)
Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer pair distance distribution function Rg: 1.7 nm 0 Dmax: 5.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer GROMACS model
SAXS data from solutions of Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer 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 = 1.54 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 25°C. 10 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.

Point mutant M65I of EVH1 domain of Homer protein homolog 1 from mouse monomer (EVH1 Homer M65I)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   13.7 kDa
 
UniProt   Q9Z2Y3 (3-121)
Sequence   FASTA