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

SASDGW4 – Model of the LZ1 domain of C-Jun-amino-terminal kinase-interacting protein 3 (JIP3)

C-Jun-amino-terminal kinase-interacting protein 3
MWexperimental 33 kDa
MWexpected 40 kDa
VPorod 84 nm3
log I(s) 3.80×10-2 3.80×10-3 3.80×10-4 3.80×10-5
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 3.80×10-2 Rg: 5.0 nm 0 (5.0 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: 5.4 nm 0 Dmax: 19.8 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 LZ1 domain 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