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 C222, 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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5544007PMC
http://dx.doi.org/10.1107/S2053230X17009748DOI Listing

Publication Analysis

Top Keywords

c44a
5
expression crystallographic
4
crystallographic studies
4
studies d1d2
4
domains
4
d1d2 domains
4
domains c44a
4
c44a homologous
4
homologous protein
4
protein urokinase
4

Similar Publications

Introduction: The mechanistic details of first line drug (FLD) resistance have been thoroughly explored but the genetic resistance mechanisms of second line injectables, which form the backbone of the combinatorial drug resistant tuberculosis therapy, are partially identified. This study aims to highlight the genetic and spoligotypic differences in the second line drug (SLD) resistant and sensitive ( clinical isolates from Mumbai (Western India) and Lucknow (Northern India).

Methods: The and target loci were screened in 126 isolates and spoligotyped.

View Article and Find Full Text PDF

The return to a good life after successfully resuscitated cardiac arrest may be hindered by cardiovascular morbidity, psychological distress and the consequences of anoxic brain injury. To support the return to everyday life, patients and their relatives are in need of health care follow-up with multiple focuses. Usually, this follow-up consists of at least one of three parallel tracks; cardiology for interventions and secondary prevention, post intensive care follow-up to capture and prevent consequences of the traumatic event and the ICU stay, or neurological follow-up for patients with neurological sequels.

View Article and Find Full Text PDF

Cysteine 96 of Ntcp is responsible for NO-mediated inhibition of taurocholate uptake.

Am J Physiol Gastrointest Liver Physiol

October 2013

Dept. of Biomedical Sciences, Tufts Cummings School of Veterinary Medicine, 200 Westboro Rd., North Grafton, MA, 01536.

The Na(+) taurocholate (TC) cotransporting polypeptide Ntcp/NTCP mediates TC uptake across the sinusoidal membrane of hepatocytes. Previously, we demonstrated that nitric oxide (NO) inhibits TC uptake through S-nitrosylation of a cysteine residue. Our current aim was to determine which of the eight cysteine residues of Ntcp is responsible for NO-mediated S-nitrosylation and inhibition of TC uptake.

View Article and Find Full Text PDF

Various environmental oxidative stresses are sensed by redox-sensitive regulators through cysteine thiol oxidation or modification. A few zinc-containing anti-sigma (ZAS) factors in actinomycetes have been reported to respond sensitively to thiol oxidation, among which RsrA from Streptomyces coelicolor is best characterized. It forms disulfide bonds upon oxidation and releases bound SigR to activate thiol oxidative stress response genes.

View Article and Find Full Text PDF

Although ileal and hepatic Na(+)-dependent bile acid transporters (SLC10A2 and SLC10A1 respectively) share structural similarities, the mutation of conserved amino acids often has distinct effects on them. We have identified two Cys residues in mouse Slc10a2 (Cys(51) and Cys(106)) the replacement of which by Ala remarkably reduces taurocholic acid (TCA) transport. Although Cys(51) is conserved in Slc10a1 as Cys(44), Ala substitution gave no apparent difference in TCA uptake.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!