The two non-visual arrestins engage ERK2 differently.

Perry-Hauser NA, Bennett Hopkins J, Zhuo Y, Zheng C, Perez I, Schultz KM, Vishnivetskiy SA, Kaya AI, Sharma P, Dalby KN, Young Chung K, Klug CS, Gurevich VV, Iverson TM
J Mol Biol :167465 (2022 Jan 22)
PMID: 35077767
doi: 10.1016/j.jmb.2022.167465
Submitted to SASBDB: 2021 Aug 31
Published in SASBDB:

SASDMG4 – Arrestin-3 ERK2 fusion, monomer (Arrestin-3 fused to extracellular signal-regulated kinase 2)

Arrestin-3 fused to extracellular signal-regulated kinase 2 experimental SAS data
Arrestin-3 ERK2 fusion, monomer (Arrestin-3 fused to extracellular signal-regulated kinase 2) Rg histogram
Sample: Arrestin-3 fused to extracellular signal-regulated kinase 2 monomer, 89 kDa Bos taurus/Rattus norvegicus protein
Buffer: 20 mM MOPS pH 7.5, 150 mM NaCl, 1 mM TCEP, and 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Mar 23
RgGuinier 3.6 nm
Dmax 14.0 nm

SASDMH4 – Arrestin-3 ERK2 fusion, dimer (Arrestin-3 fused to extracellular signal-regulated kinase 2)

Arrestin-3 fused to extracellular signal-regulated kinase 2 experimental SAS data
Arrestin-3 fused to extracellular signal-regulated kinase 2 Kratky plot
Sample: Arrestin-3 fused to extracellular signal-regulated kinase 2 dimer, 178 kDa Bos taurus/Rattus norvegicus protein
Buffer: 20 mM MOPS pH 7.5, 150 mM NaCl, 1 mM TCEP, and 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Mar 23
RgGuinier 4.3 nm
Dmax 16.0 nm