5yy8
From Proteopedia
Crystal structure of the Kelch domain of human NS1-BP
Structural highlights
Function[NS1BP_HUMAN] Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization; Protects neurons from dendritic spines and actin filaments damage induced by the actin-destabilizing cytochalasin B when overexpressed. Activates Erk signaling pathway when overexpressed in cultured cell lines (By similarity). May be a component of the cellular splicing machinery with a role in pre-mRNA splicing; may mediate the inhibition of splicing by NS/influenza virus NS1A protein. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription.[1] Publication Abstract from PubMedNS1-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 A resolution. The Kelch domain adopts a highly symmetric six-bladed beta-propeller fold structure. Each blade of the beta-propeller is composed of four antiparallel beta-strands. Comparison of the Kelch-domain structures of NS1-BP and its homologues showed that the Gly-Gly pair in beta-strand B and the hydrophobic Trp residue in beta-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. Crystal structure of the Kelch domain of human NS1-binding protein at 1.98 A resolution.,Guo L, Liu Y Acta Crystallogr F Struct Biol Commun. 2018 Mar 1;74(Pt 3):174-178. doi:, 10.1107/S2053230X18001577. Epub 2018 Feb 26. PMID:29497022[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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