1h0c

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Revision as of 19:28, 29 October 2007 by OCA (talk | contribs) (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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File:1h0c.gif


1h0c, resolution 2.50Å

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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 [[1]], with EC number [2.6.1.44]. 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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