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Expression and crystallographic studies of the D1D2 domains of C4.4A, a homologous protein to the urokinase receptor
Author(s) -
Chen Shanli,
Lin Lin,
Yuan Cai,
Gårdsvoll Henrik,
Kriegbaum Mette C.,
Ploug Michael,
Huang Mingdong
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17009748
Subject(s) - proteolysis , biomarker , urokinase receptor , receptor , chemistry , crystallization , crystallography , biology , microbiology and biotechnology , biophysics , biochemistry , enzyme , organic chemistry
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 C 222 1 , 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.