Structural basis for specific RNA recognition by the alternative splicing factor RBM5.

Soni K, Jagtap PKA, Martínez-Lumbreras S, Bonnal S, Geerlof A, Stehle R, Simon B, Valcárcel J, Sattler M, Nat Commun 14(1):4233 (2023) Europe PMC

SASDM53 – RRM1-ZnF1-RRM2 triple domains of RNA-binding protein 5 (C191G mutant)

RNA Binding Motif protein 5 (I107T, C191G)
MWexperimental 24 kDa
MWexpected 26 kDa
VPorod 36 nm3
log I(s) 6.92×10-1 6.92×10-2 6.92×10-3 6.92×10-4
RNA Binding Motif protein 5 (I107T, C191G) small angle scattering data  s, nm-1
ln I(s)
RNA Binding Motif protein 5 (I107T, C191G) Guinier plot ln 6.92×10-1 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
RNA Binding Motif protein 5 (I107T, C191G) Kratky plot 1.104 0 √3 sRg
p(r)
RNA Binding Motif protein 5 (I107T, C191G) pair distance distribution function Rg: 2.4 nm 0 Dmax: 7.8 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of the RRM1-ZnF1-RRM2 triple domains of RNA-binding protein 5 (C191G mutant) in 20 mM MES, 400 mM NaCl, 1 mM DTT, pH 6.5 were collected using a Rigaku BioSAXS-1000 instrument (SFB 1035, Technische Universität München, Garching, Germany) equipped with a Pilatus 100K detector at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 5°C. Eight successive 900 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

RNA Binding Motif protein 5 (I107T, C191G) (RBM5 (I107T, C191G))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   25.5 kDa
 
UniProt   P52756 (94-315)
Sequence   FASTA