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| | <StructureSection load='5yy8' size='340' side='right'caption='[[5yy8]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='5yy8' size='340' side='right'caption='[[5yy8]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yy8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YY8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YY8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yy8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YY8 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.979Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yy8 OCA], [http://pdbe.org/5yy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yy8 RCSB], [http://www.ebi.ac.uk/pdbsum/5yy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yy8 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yy8 OCA], [https://pdbe.org/5yy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yy8 RCSB], [https://www.ebi.ac.uk/pdbsum/5yy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yy8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NS1BP_HUMAN 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.<ref>PMID:16582008</ref> | + | [https://www.uniprot.org/uniprot/NS1BP_HUMAN 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.<ref>PMID:16582008</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, L]] | + | [[Category: Guo L]] |
| - | [[Category: Liang, H]] | + | [[Category: Liang H]] |
| - | [[Category: Liu, Y]] | + | [[Category: Liu Y]] |
| - | [[Category: Host-virus interaction]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| 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 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
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