Expression and crystallographic studies of the D1D2 domains of C4.4A, a homologous protein to the urokinase receptor

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C4.4A is a glycosylphosphatidylinositol-anchored membrane protein comprised of two LU domains (Ly6/uPAR-like domains) and an extensively O-glycosylated C-terminal Ser/Thr/Pro-rich region. C4.4A is a novel biomarker for squamous epithelial differentiation. Its expression is dysregulated under various pathological conditions and it is a robust biomarker for poor prognosis in various malignant conditions such as pulmonary adenocarcinoma. To facilitate crystallization, the two LU domains were excised from intact C4.4A by limited proteolysis, purified and crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 2.7 Å resolution and belonged to space group C2221, with unit-cell parameters a = 55.49, b = 119.63, c = 168.54 Å. The statistics indicated good quality of the data, which form a solid basis for the determination of the C4.4A structure.The two amino-terminal LU domains of C4.4A were excised by limited proteolysis and were crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to 2.7 Å resolution, giving good-quality data.

Original languageEnglish
JournalActa Crystallographica Section F: Structural Biology Communications
Volume73
Issue number8
Pages (from-to)486-490
Number of pages5
ISSN2053-230X
DOIs
Publication statusPublished - 1 Aug 2017

    Research areas

  • C4.4A, glycosylation, LU domains, prognostic cancer biomarkers

ID: 185277329