Selective cargo and membrane recognition by SNX17 regulates its interaction with Retriever

Martín-González A, Méndez-Guzmán I, Zabala-Zearreta M, Quintanilla A, García-López A, Martínez-Lombardía E, Albesa-Jové D, Acosta J, Lucas M, EMBO Reports (2024) DOI

SASDVR6 – Vacuolar protein sorting-associated protein 26C (VPS26C)

Vacuolar protein sorting-associated protein 26C
MWexperimental 33 kDa
MWexpected 33 kDa
VPorod 44 nm3
log I(s) 1.95×10-2 1.95×10-3 1.95×10-4 1.95×10-5
Vacuolar protein sorting-associated protein 26C small angle scattering data  s, nm-1
ln I(s)
Vacuolar protein sorting-associated protein 26C Guinier plot ln 1.95×10-2 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Vacuolar protein sorting-associated protein 26C Kratky plot 1.104 0 √3 sRg
p(r)
Vacuolar protein sorting-associated protein 26C pair distance distribution function Rg: 2.7 nm 0 Dmax: 9.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Vacuolar protein sorting-associated protein 26C ALPHAFOLD model
log I(s)
 s, nm-1
Vacuolar protein sorting-associated protein 26C DAMMIN model
Synchrotron SAXS data from solutions of VPS26C in 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.0954 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 48.00 μl sample at 5 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW403-4F column at 25°C. 620 successive 1 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.

Vacuolar protein sorting-associated protein 26C (VPS26C)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   33.0 kDa
 
UniProt   O14972 (1-297)
Sequence   FASTA