We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5yy8

From Proteopedia

Jump to: navigation, search

Crystal structure of the Kelch domain of human NS1-BP

Structural highlights

5yy8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.979Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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 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

↑ Dunham EE, Stevens EA, Glover E, Bradfield CA. The aryl hydrocarbon receptor signaling pathway is modified through interactions with a Kelch protein. Mol Pharmacol. 2006 Jul;70(1):8-15. Epub 2006 Mar 31. PMID:16582008 doi:http://dx.doi.org/mol.106.024380
↑ Guo L, Liu Y. Crystal structure of the Kelch domain of human NS1-binding protein at 1.98 A resolution. Acta Crystallogr F Struct Biol Commun. 2018 Mar 1;74(Pt 3):174-178. doi:, 10.1107/S2053230X18001577. Epub 2018 Feb 26. PMID:29497022 doi:http://dx.doi.org/10.1107/S2053230X18001577