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Rigshospitalet - a part of Copenhagen University Hospital
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Expression and crystallographic studies of the D1D2 domains of C4.4A, a homologous protein to the urokinase receptor

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  4. Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond?

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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.

Original languageEnglish
JournalActa crystallographica. Section F, Structural biology communications
Volume73
Issue numberPt 8
Pages (from-to)486-490
Number of pages5
ISSN2053-230X
DOIs
Publication statusPublished - 1 Aug 2017

    Research areas

  • Amino Acid Sequence, Animals, Biomarkers, Tumor, Cell Adhesion Molecules, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Drosophila melanogaster, GPI-Linked Proteins, Gene Expression, Genetic Vectors, Humans, Protein Domains, Receptors, Urokinase Plasminogen Activator, Recombinant Proteins, Sequence Deletion, Sequence Homology, Amino Acid, X-Ray Diffraction, Journal Article

ID: 52425594