Linked Life Data

18348864

Source:http://linkedlifedata.com/resource/pubmed/id/18348864

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-4-15
pubmed:abstractText
GD3-synthase is a sialyltransferase that catalyzes the synthesis of ganglioside GD3 leading to the b- and c-series gangliosides. It contains four common sequence regions of vertebrate sialyltransferases, referred to as the L, S, III, and VS sialylmotifs, which have been identified in all vertebrate sialyltransferases that play important roles in spatial structure maintenance and protein functions. No 3D structural information, however, is currently available for vertebrate sialyltransferases. Using primary sequence of human GD3-synthase, we identified the structure of a prokaryotic sialyltransferase (CstII, also known as an alpha2,3/alpha2,8-sialyltransferase) as the template for protein homology modeling. Secondary structural alignment between these two proteins identified several conserved amino-acid residues. The functions of four conserved residues (Asn(188), Pro(189), Ser(190), and Arg(272)) between the L and S sialylmotifs in human GD3-synthase were investigated using mutational analysis and molecular modeling, and it was found that these sites are involved in determining the alpha2,8-linkage specificity of GD3-synthase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
23
pubmed:volume
370
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-71
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Identification and analysis of novel functional sites in human GD3-synthase.
pubmed:affiliation
Institute of Molecular Medicine and Genetics, Medical College of Georgia, 1120 15th Street, Augusta, GA 30912, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural