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

Authors

Toshiyuki Hamada, 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 α‐ and two single‐turn 310‐helices and two β‐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.

Digital Object Identifier (DOI)

10.1110/ps.051700406 About DOI

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