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

Authors :
Hamada, Toshiyuki
Ito, Yoko
Abe, Takamasa
Hayashi, Fumiaki
Güntert, Peter
Inoue, Makoto
Kigawa, Takanori
Terada, Takaho
Shirouzu, Mikako
Yoshida, Mayumi
Tanaka, Akiko
Sugano, Sumio
Yokoyama, Shigeyuki
Hirota, Hiroshi
Source :
Protein Science: A Publication of the Protein Society; 2006, Vol. 15 Issue 5, p1010-1016, 7p
Publication Year :
2006

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 3<subscript>10</subscript>-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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09618368
Volume :
15
Issue :
5
Database :
Complementary Index
Journal :
Protein Science: A Publication of the Protein Society
Publication Type :
Academic Journal
Accession number :
90754990
Full Text :
https://doi.org/10.1110/ps.051700406