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Acta Crystallogr F Struct Biol Commun. 2018 Mar 1;74(Pt 3):174-178. doi: 10.1107/S2053230X18001577. Epub 2018 Feb 26.
Crystal structure of the Kelch domain of human NS1-binding protein at 1.98 ? resolution.
Guo L1, Liu Y1.
Author information
Abstract
NS1-binding protein (NS1-BP), which belongs to the Kelch protein superfamily, was first identified as a novel human 70 kDa protein that interacts with NS1 of Influenza A virus. It is involved in many cell functions, including pre-mRNA splicing, the ERK signalling pathway, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitylation. However, the structure of NS1-BP is still unknown, which may impede functional studies. Here, the structure of the C-terminal Kelch domain of NS1-BP (NS1-BP-C; residues 330-642) was determined at 1.98 ? resolution. The Kelch domain adopts a highly symmetric six-bladed β-propeller fold structure. Each blade of the β-propeller is composed of four antiparallel β-strands. Comparison of the Kelch-domain structures of NS1-BP and its homologues showed that the Gly-Gly pair in β-strand B and the hydrophobic Trp residue in β-strand D are highly conserved, while the B-C loops in blades 2 and 6 are variable. This structure of the Kelch domain of NS1-BP extends the understanding of NS1-BP.
KEYWORDS:
ERK signalling pathway; F-actin organization; Kelch domain; NS1-binding protein; X-ray crystallography; aryl hydrocarbon receptor (AHR) pathway; pre-mRNA splicing; protein ubiquitylation
PMID: 29497022 DOI: 10.1107/S2053230X18001577
Crystal structure of the Kelch domain of human NS1-binding protein at 1.98 ? resolution.
Guo L1, Liu Y1.
Author information
Abstract
NS1-binding protein (NS1-BP), which belongs to the Kelch protein superfamily, was first identified as a novel human 70 kDa protein that interacts with NS1 of Influenza A virus. It is involved in many cell functions, including pre-mRNA splicing, the ERK signalling pathway, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitylation. However, the structure of NS1-BP is still unknown, which may impede functional studies. Here, the structure of the C-terminal Kelch domain of NS1-BP (NS1-BP-C; residues 330-642) was determined at 1.98 ? resolution. The Kelch domain adopts a highly symmetric six-bladed β-propeller fold structure. Each blade of the β-propeller is composed of four antiparallel β-strands. Comparison of the Kelch-domain structures of NS1-BP and its homologues showed that the Gly-Gly pair in β-strand B and the hydrophobic Trp residue in β-strand D are highly conserved, while the B-C loops in blades 2 and 6 are variable. This structure of the Kelch domain of NS1-BP extends the understanding of NS1-BP.
KEYWORDS:
ERK signalling pathway; F-actin organization; Kelch domain; NS1-binding protein; X-ray crystallography; aryl hydrocarbon receptor (AHR) pathway; pre-mRNA splicing; protein ubiquitylation
PMID: 29497022 DOI: 10.1107/S2053230X18001577