5YY8

Crystal structure of the Kelch domain of human NS1-BP

Summary for 5YY8

• Entry DOI: 10.2210/pdb5yy8/pdb
• Descriptor: Influenza virus NS1A-binding protein (2 entities in total)
• Functional Keywords: host-virus interaction, protein binding
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : Q9Y6Y0
• Total number of polymer chains: 1
• Total formula weight: 37030.34

Authors

Guo, L.,Liu, Y.,Liang, H. (deposition date: 2017-12-08, release date: 2018-03-14, Last modification date: 2024-10-16)

Primary citation

Guo, L.,Liu, Y.
Crystal structure of the Kelch domain of human NS1-binding protein at 1.98 angstrom resolution.
Acta Crystallogr F Struct Biol Commun, 74:174-178, 2018

PubMed 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 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.

PubMed: 29497022
DOI: 10.1107/S2053230X18001577

Experimental method

X-RAY DIFFRACTION (1.979 Å)