Structural characterization of the RH1-LZI tandem of JIP3/4 highlights RH1 domains as a cytoskeletal motor-binding motif.

Vilela F, Velours C, Chenon M, Aumont-Nicaise M, Campanacci V, Thureau A, Pylypenko O, Andreani J, Llinas P, Ménétrey J, Sci Rep 9(1):16036 (2019) Europe PMC

SASDGV4 – Model of the RH1-LZ1 domains of C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)

C-Jun-amino-terminal kinase-interacting protein 3
MWexperimental 42 kDa
MWexpected 40 kDa
VPorod 140 nm3
log I(s) 5.50×10-2 5.50×10-3 5.50×10-4 5.50×10-5
C-Jun-amino-terminal kinase-interacting protein 3 small angle scattering data  s, nm-1
ln I(s)
C-Jun-amino-terminal kinase-interacting protein 3 Guinier plot ln 5.50×10-2 Rg: 6.3 nm 0 (6.3 nm)-2 s2
(sRg)2I(s)/I(0)
C-Jun-amino-terminal kinase-interacting protein 3 Kratky plot 1.104 0 √3 sRg
p(r)
C-Jun-amino-terminal kinase-interacting protein 3 pair distance distribution function Rg: 6.6 nm 0 Dmax: 23.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
C-Jun-amino-terminal kinase-interacting protein 3 OTHER model
Synchrotron SAXS data from solutions of the RH1-LZ1 domains of JIP3 in 20 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH 7.1 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 6 mg/ml was injected at a 0.30 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Number of frames = UNKNOWN

C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   20.0 kDa
 
UniProt   Q9UPT6 (22-187)
Sequence   FASTA