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Region Hovedstaden - en del af Københavns Universitetshospital
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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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DOI

  1. Evolution and Medical Significance of LU Domain-Containing Proteins

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

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  3. Origin and diversification of the plasminogen activation system among chordates

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  4. GPIHBP1 autoantibody syndrome during interferon β1a treatment

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  5. Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis

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Vis graf over relationer

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.

OriginalsprogEngelsk
TidsskriftActa crystallographica. Section F, Structural biology communications
Vol/bind73
Udgave nummerPt 8
Sider (fra-til)486-490
Antal sider5
ISSN2053-230X
DOI
StatusUdgivet - 1 aug. 2017

ID: 52425594