1wvo: Difference between revisions

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[[Image:1wvo.gif|left|200px]]<br />

[[Image:1wvo.gif|left|200px]]<br /><applet load="1wvo" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1wvo" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1wvo" />

'''Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA].

1WVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA].

==Reference==

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[[Category: Hirota, H.]]

[[Category: Ito, Y.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Yokoyama, S.]]

[[Category: antifreeze protein like domain]]

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[[Category: structural genomics]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 19~~:55:~~23 2007~~''

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@@ Line 1: / Line 1: @@
-[[Image:1wvo.gif|left|200px]]<br />
+[[Image:1wvo.gif|left|200px]]<br /><applet load="1wvo" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1wvo" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1wvo" />
 '''Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.'''<br />
 ==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.
+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==
-WVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA].
+WVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVO OCA].
 ==Reference==
@@ Line 18: / Line 17: @@
 [[Category: Hirota, H.]]
 [[Category: Ito, Y.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Yokoyama, S.]]
 [[Category: antifreeze protein like domain]]
@@ Line 29: / Line 28: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:55:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:44 2008''