Solution structure of the antifreeze-like domain of human sialic acid synthase

Protein Sci. 2006 May;15(5):1010-6. doi: 10.1110/ps.051700406. Epub 2006 Apr 5.

Abstract

The structure of the C-terminal antifreeze-like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one alpha- and two single-turn 3(10)-helices and two beta-strands, and is similar to those of the type III antifreeze proteins. Evolutionary trace analyses of the type III antifreeze protein family suggested that the class-specific residues in the human and bacterial AFL domains are important for their substrate binding, while the class-specific residues of the fish antifreeze proteins are gathered on the ice-binding surface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antifreeze Proteins, Type III / chemistry*
  • Evolution, Molecular
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Oxo-Acid-Lyases / chemistry*
  • Phylogeny
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Solutions
  • Structure-Activity Relationship

Substances

  • Antifreeze Proteins, Type III
  • Solutions
  • N-acetylneuraminate synthase
  • Oxo-Acid-Lyases