1h0c: Difference between revisions
New page: left|200px<br /> <applet load="1h0c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h0c, resolution 2.50Å" /> '''THE CRYSTAL STRUCTU... |
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==About this Structure== | ==About this Structure== | ||
1H0C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with PLP, AOA and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H0C OCA]]. | 1H0C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with PLP, AOA and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alanine--glyoxylate_transaminase Alanine--glyoxylate transaminase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H0C OCA]]. | ||
==Reference== | ==Reference== | ||
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1., Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ, J Mol Biol. 2003 Aug 15;331(3):643-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12899834 12899834] | Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1., Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ, J Mol Biol. 2003 Aug 15;331(3):643-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12899834 12899834] | ||
[[Category: Alanine--glyoxylate transaminase]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 12:49, 30 October 2007
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THE CRYSTAL STRUCTURE OF HUMAN ALANINE:GLYOXYLATE AMINOTRANSFERASE
OverviewOverview
A deficiency of the liver-specific enzyme alanine:glyoxylate, aminotransferase (AGT) is responsible for the potentially lethal, hereditary kidney stone disease primary hyperoxaluria type 1 (PH1). Many, of the mutations in the gene encoding AGT are associated with specific, enzymatic phenotypes such as accelerated proteolysis (Ser205Pro), intra-peroxisomal aggregation (Gly41Arg), inhibition of pyridoxal, phosphate binding and loss of catalytic activity (Gly82Glu), and, peroxisome-to-mitochondrion mistargeting (Gly170Arg). Several mutations, including that responsible for AGT mistargeting, co-segregate and interact, synergistically with a Pro11Leu polymorphism found at high frequency in, the normal population. In order to gain further insights into the, mechanistic link between genotype and ... [(full description)]
About this StructureAbout this Structure
1H0C is a [Single protein] structure of sequence from [Homo sapiens] with PLP, AOA and GOL as [ligands]. Active as [Alanine--glyoxylate transaminase], with EC number [2.6.1.44]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1., Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ, J Mol Biol. 2003 Aug 15;331(3):643-52. PMID:12899834
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