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

Expression and crystallographic studies of the D1D2 domains of C4.4A, a homologous protein to the... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17009748
pmid
28777093
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ; ;

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