About: Crystal Structure of the N-Acetylmannosamine Kinase Domain of GNE

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About: Crystal Structure of the N-Acetylmannosamine Kinase Domain of GNE Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Crystal Structure of the N-Acetylmannosamine Kinase Domain of GNE
Creator	Mackenzie, Farrell Nedyalkova, Lyudmila Park, Hee-Won Tempel, Wolfram Tong, Yufeng
topic	covid:178363fb71ad0ae91e621e6e51fc03bb521f5695#this
source	PMC
abstract	BACKGROUND: UDP-GlcNAc 2-epimerase/ManNAc 6-kinase, GNE, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. PRINCIPAL FINDINGS: We solved the structure of the GNE kinase domain in the ligand-free state. The protein exists predominantly as a dimer in solution, with small populations of monomer and higher-order oligomer in equilibrium with the dimer. Crystal packing analysis reveals the existence of a crystallographic hexamer, and that the kinase domain dimerizes through the C-lobe subdomain. Mapping of disease-related missense mutations onto the kinase domain structure revealed that the mutation sites could be classified into four different groups based on the location – dimer interface, interlobar helices, protein surface, or within other secondary structural elements. CONCLUSIONS: The crystal structure of the kinase domain of GNE provides a structural basis for understanding disease-causing mutations and a model of hexameric wild type full length enzyme. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.
has issue date	2009-10-20(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0007165
bibo:pmid	19841673
has license	cc-by
sha1sum (hex)	178363fb71ad0ae91e621e6e51fc03bb521f5695
schema:url	https://doi.org/10.1371/journal.pone.0007165
resource representing a document's title	Crystal Structure of the N-Acetylmannosamine Kinase Domain of GNE
has PubMed Central identifier	PMC2742894
has PubMed identifier	19841673
schema:publication	PLoS One
resource representing a document's body	covid:178363fb71ad0ae91e621e6e51fc03bb521f5695#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/178363fb71ad0ae91e621e6e51fc03bb521f5695
is schema:about of	named entity 'GNE' named entity 'autosomal recessive' named entity 'enzyme' named entity 'ENZYME' named entity 'MYOPATHY' named entity 'KEY' named entity 'ROLE' named entity 'ROK' named entity 'CRYSTAL STRUCTURE' named entity 'GNE' named entity 'N-ACETYLMANNOSAMINE KINASE' named entity 'FUNCTIONAL' named entity 'GNE' named entity 'AUTOSOMAL RECESSIVE' named entity 'PLAYS' named entity 'GLCNAC 2-EPIMERASE' named entity 'FAMILY' named entity 'BELONGING' named entity 'UDP-GLCNAC' named entity 'BACKGROUND' named entity 'PROTEIN ' named entity 'KINASE DOMAIN' named entity 'MUTATIONS' named entity 'CONTAINS' named entity 'IS A' named entity 'INCLUSION BODY MYOPATHY' named entity 'KINASE DOMAIN' named entity 'HUMAN PROTEIN' named entity 'CAUSE' named entity 'ORF' named entity 'SIALIC ACID BIOSYNTHESIS' named entity 'KINASE' named entity 'ROK' named entity 'GNE' named entity 'inclusion body myopathy' named entity 'protein' named entity 'kinase' named entity 'biosynthesis' named entity 'autosomal recessive' named entity 'ORF' named entity 'Mutations' named entity 'repressor' named entity 'dimerize' named entity 'kinase' named entity 'gene' named entity 'Relative solvent accessibility' named entity 'binding site' named entity 'epimerase' named entity 'wavelength' named entity 'metabolism' named entity 'vertebrate' named entity 'Bacillus subtilis' named entity 'ATPase' named entity 'free energy' named entity 'glycerol' named entity 'Qiagen' named entity 'sodium citrate' named entity 'autosomal recessive' named entity 'epimerase' named entity 'zinc-binding motif' named entity 'substrate binding' named entity 'sugar' named entity 'vector' named entity 'gel filtration' named entity 'mutation' named entity 'dimerization' named entity 'SeMet' named entity 'solvation' named entity 'eluted' named entity 'UDP-GlcNAc' named entity 'homologous structure' named entity 'mutation' named entity 'helix' named entity 'human genome' named entity 'transcriptional repressor'

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