The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat.

Ortega E, Buey RM, Sonnenberg A, de Pereda JM, J Biol Chem 286(14):12429-38 (2011) Europe PMC

SASDAS6 – Plectin, fragment of the plakin domain encompassing the spectrin repeats SR3-SR4-SR5 and the SH3

Plectin
MWexperimental 38 kDa
MWexpected 43 kDa
VPorod 57 nm3
log I(s) 2.37×101 2.37×100 2.37×10-1 2.37×10-2
Plectin small angle scattering data  s, nm-1
ln I(s)
Plectin Guinier plot ln 2.37×101 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
Plectin Kratky plot 1.104 0 √3 sRg
p(r)
Plectin pair distance distribution function Rg: 4.2 nm 0 Dmax: 14.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Plectin DAMMIF model
Synchrotron SAXS data from solutions of Plectin, fragment of the plakin domain encompassing the spectrin repeats SR3-SR4-SR5 and the SH3 in 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 2.5 mM DTT, pH 7.5 were collected on the cSAXS beam line at the Swiss Light Source storage ring (Villigen, Switzerland) using a Pilatus 2M detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.2 and 9.6 mg/ml were measured at 10°C. 60 successive 0.500 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Use of SAXS to analyze the structure of central region of the plakin domain of plectin.

Plectin
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   42.9 kDa
 
UniProt   Q15149
Sequence   FASTA