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Publication Abstract from PubMed

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.

Solution structure of the antifreeze-like domain of human sialic acid synthase.,Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. PMID:16597820^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.