2qlr
From Proteopedia
(New page: 200px<br /><applet load="2qlr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qlr, resolution 2.30Å" /> '''Crystal structure of...) |
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caption="2qlr, resolution 2.30Å" /> | caption="2qlr, resolution 2.30Å" /> | ||
'''Crystal structure of human kynurenine aminotransferase II'''<br /> | '''Crystal structure of human kynurenine aminotransferase II'''<br /> | ||
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| + | ==Overview== | ||
| + | Human kynurenine aminotransferase II (hKAT-II) efficiently catalyzes the transamination of knunrenine to kynurenic acid (KYNA). KYNA is the only known endogenous antagonist of N-methyl-d-aspartate (NMDA) receptors and is also an antagonist of 7-nicotinic acetylcholine receptors. Abnormal concentrations of brain KYNA have been implicated in the pathogenesis and development of several neurological and psychiatric diseases in humans. Consequently, enzymes involved in the production of brain KYNA have been considered potential regulatory targets. In this article, we report a 2.16A crystal structure of hKAT-II and a 1.95A structure of its complex with kynurenine. The protein architecture of hKAT-II reveals that it belongs to the fold-type I pyridoxal 5-phosphate (PLP)-dependent enzymes. In comparison with all subclasses of fold-type I-PLP-dependent enzymes, we propose that hKAT-II represents a novel subclass in the fold-type I enzymes because of the unique folding of its first 65 N-terminal residues. This study provides a molecular basis for future effort in maintaining physiological concentrations of KYNA through molecular and biochemical regulation of hKAT-II. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2QLR 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 <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLR OCA]. | + | 2QLR 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 <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+426'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Residue+A+427'>AC2</scene>, <scene name='pdbsite=AC3:Gol+Binding+Site+For+Residue+B+426'>AC3</scene>, <scene name='pdbsite=AC4:Gol+Binding+Site+For+Residue+C+427'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+C+428'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Residue+C+429'>AC6</scene>, <scene name='pdbsite=AC7:Gol+Binding+Site+For+Residue+C+430'>AC7</scene>, <scene name='pdbsite=AC8:Gol+Binding+Site+For+Residue+D+426'>AC8</scene>, <scene name='pdbsite=AC9:Gol+Binding+Site+For+Residue+D+427'>AC9</scene>, <scene name='pdbsite=BC1:Gol+Binding+Site+For+Residue+D+428'>BC1</scene> and <scene name='pdbsite=BC2:Gol+Binding+Site+For+Residue+D+429'>BC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLR OCA]. |
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| + | ==Reference== | ||
| + | Crystal Structure of Human Kynurenine Aminotransferase II., Han Q, Robinson H, Li J, J Biol Chem. 2008 Feb 8;283(6):3567-73. Epub 2007 Dec 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18056995 18056995] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:20 2008'' |
Revision as of 16:40, 21 February 2008
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Crystal structure of human kynurenine aminotransferase II
Overview
Human kynurenine aminotransferase II (hKAT-II) efficiently catalyzes the transamination of knunrenine to kynurenic acid (KYNA). KYNA is the only known endogenous antagonist of N-methyl-d-aspartate (NMDA) receptors and is also an antagonist of 7-nicotinic acetylcholine receptors. Abnormal concentrations of brain KYNA have been implicated in the pathogenesis and development of several neurological and psychiatric diseases in humans. Consequently, enzymes involved in the production of brain KYNA have been considered potential regulatory targets. In this article, we report a 2.16A crystal structure of hKAT-II and a 1.95A structure of its complex with kynurenine. The protein architecture of hKAT-II reveals that it belongs to the fold-type I pyridoxal 5-phosphate (PLP)-dependent enzymes. In comparison with all subclasses of fold-type I-PLP-dependent enzymes, we propose that hKAT-II represents a novel subclass in the fold-type I enzymes because of the unique folding of its first 65 N-terminal residues. This study provides a molecular basis for future effort in maintaining physiological concentrations of KYNA through molecular and biochemical regulation of hKAT-II.
About this Structure
2QLR is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Sites: , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Crystal Structure of Human Kynurenine Aminotransferase II., Han Q, Robinson H, Li J, J Biol Chem. 2008 Feb 8;283(6):3567-73. Epub 2007 Dec 5. PMID:18056995
Page seeded by OCA on Thu Feb 21 18:40:20 2008
