1wvo
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(New page: 200px<br /> <applet load="1wvo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvo" /> '''Solution structure of RSGI RUH-029, an anti...)
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Revision as of 17:48, 12 November 2007
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Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.
Overview
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.
About this Structure
1WVO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 19:55:23 2007
Categories: Homo sapiens | Single protein | Hamada, T. | Hayashi, F. | Hirota, H. | Ito, Y. | RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative. | Yokoyama, S. | Antifreeze protein like domain | N-acetylneuraminic acid phosphate synthase | National project on protein structural and functional analyses | Nmr | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics