| Literature DB >> 16597820 |
Toshiyuki Hamada1, Yoko Ito, Takamasa Abe, Fumiaki Hayashi, Peter Güntert, Makoto Inoue, Takanori Kigawa, Takaho Terada, Mikako Shirouzu, Mayumi Yoshida, Akiko Tanaka, Sumio Sugano, Shigeyuki Yokoyama, Hiroshi Hirota.
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.Entities:
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Year: 2006 PMID: 16597820 PMCID: PMC2242509 DOI: 10.1110/ps.051700406
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725