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Fig. 1 | BMC Biology

Fig. 1

From: Oligomeric interface modulation causes misregulation of purine 5´-nucleotidase in relapsed leukemia

Fig. 1

Oligomerization and thermostability of ALL-specific cN-II mutants. a Distribution of the identified mutations within the 3D structure of cN-II (Protein Data Bank [PDB] ID 2XCX; missing loops were modeled using the ModLoop server). The mutants studied in this work (R367Q, R238W and L375F) are highlighted using a boldface font and thick lines. Each subunit is represented in a different color. b Thermostability of cN-II proteins studied by differential scanning fluorimetry. Each sample was measured twice in two independent measurements. c Size exclusion chromatography of full-length cN-II protein. Elution volumes together with estimated molecular weight are summarized in the table (e). d Blue native polyacrylamide gel electrophoresis (BN-PAGE) of the studied full-length proteins. The protein samples (5 μg) were loaded as follows: M molecular weight standard, S β-amylase from sweet potato (200 kDa), 1 wild type, 2 R367Q, 3 R238W, 4 L375F. e Table summarizing data for the cN-II variants obtained from size exclusion chromatography and small-angle X-ray scattering (SAXS). Analysis of proteins with 1 mg/ml concentration is shown. The values of Rg and MWGuinier were calculated by Guinier approximation; Dmax and Porod volume were determined using fitting of distance distribution functions

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