Crystal structure of the Kelch domain of human NS1-binding protein at 1.98   Å resolution

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   Å 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.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: NS1-binding protein Kelch domain ERK signalling pathway pre-mRNA splicing aryl hydrocarbon receptor (AHR) pathway F-actin organization protein ubiquitylation X-ray crystallography research communications Source Type: research