Identification and analysis of novel functional sites in human GD3-synthase

Yihua Gu, Robert K. Yu

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

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 α2,3/α2,8-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 (Asn188, Pro189, Ser190, and Arg272) 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 α2,8-linkage specificity of GD3-synthase.

Original languageEnglish (US)
Pages (from-to)67-71
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume370
Issue number1
DOIs
StatePublished - May 23 2008

Fingerprint

Sialyltransferases
Vertebrates
Proteins
Molecular modeling
Gangliosides
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase
Maintenance
Amino Acids

Keywords

  • Functional site
  • GD3-synthase
  • Molecular modeling
  • Sialyltransferase
  • Site-directed mutagenesis

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification and analysis of novel functional sites in human GD3-synthase. / Gu, Yihua; Yu, Robert K.

In: Biochemical and Biophysical Research Communications, Vol. 370, No. 1, 23.05.2008, p. 67-71.

Research output: Contribution to journalArticle

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