5yy8

From Proteopedia

(Difference between revisions)

Revision as of 06:28, 14 March 2018

Crystal structure of the Kelch domain of human NS1-BP

Structural highlights

5yy8 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5yy8"

Categories: Guo, L | Liang, H | Liu, Y | Host-virus interaction | Protein binding

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5yy8 is ON HOLD
+==Crystal structure of the Kelch domain of human NS1-BP==
+<StructureSection load='5yy8' size='340' side='right' caption='[[5yy8]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
+== 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://oca.weizmann.ac.il/oca-docs/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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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>
+</table>
+== 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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Guo, L., Liu, Y., Liang, H.
+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<ref>PMID:29497022</ref>
-Description: Crystal structure of the Kelch domain of human NS1-BP
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5yy8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Guo, L]]
 [[Category: Liang, H]]
 [[Category: Liu, Y]]
+[[Category: Host-virus interaction]]
+[[Category: Protein binding]]

5yy8

From Proteopedia

Revision as of 06:28, 14 March 2018

Crystal structure of the Kelch domain of human NS1-BP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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