2r2n
From Proteopedia
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| - | [[Image:2r2n.jpg|left|200px]] | + | [[Image:2r2n.jpg|left|200px]] |
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| - | '''The crystal structure of human kynurenine aminotransferase II in complex with kynurenine''' | + | {{Structure |
| + | |PDB= 2r2n |SIZE=350|CAPTION= <scene name='initialview01'>2r2n</scene>, resolution 1.95Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Pmp+Binding+Site+For+Residue+A+426'>AC1</scene>, <scene name='pdbsite=AC2:Pmp+Binding+Site+For+Residue+B+426'>AC2</scene>, <scene name='pdbsite=AC3:Pmp+Binding+Site+For+Residue+C+426'>AC3</scene>, <scene name='pdbsite=AC4:Pmp+Binding+Site+For+Residue+D+426'>AC4</scene>, <scene name='pdbsite=AC5:Kyn+Binding+Site+For+Residue+A+427'>AC5</scene>, <scene name='pdbsite=AC6:Kyn+Binding+Site+For+Residue+C+427'>AC6</scene>, <scene name='pdbsite=AC7:Kyn+Binding+Site+For+Residue+A+428'>AC7</scene>, <scene name='pdbsite=AC8:Kyn+Binding+Site+For+Residue+C+428'>AC8</scene>, <scene name='pdbsite=AC9:Gol+Binding+Site+For+Residue+D+427'>AC9</scene>, <scene name='pdbsite=BC1:Gol+Binding+Site+For+Residue+C+429'>BC1</scene>, <scene name='pdbsite=BC2:Gol+Binding+Site+For+Residue+D+428'>BC2</scene>, <scene name='pdbsite=BC3:Gol+Binding+Site+For+Residue+D+429'>BC3</scene>, <scene name='pdbsite=BC4:Gol+Binding+Site+For+Residue+D+430'>BC4</scene> and <scene name='pdbsite=BC5:Gol+Binding+Site+For+Residue+A+429'>BC5</scene> | ||
| + | |LIGAND= <scene name='pdbligand=PMP:4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE'>PMP</scene>, <scene name='pdbligand=KYN:KYNURENINE'>KYN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= AADAT, KAT2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of human kynurenine aminotransferase II in complex with kynurenine''' | ||
| + | |||
| + | |||
| + | ==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== | ||
| - | 2R2N is a [ | + | 2R2N is a [[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=2R2N 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:[http://www.ncbi.nlm.nih.gov/pubmed/18056995 18056995] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Han, Q.]] | [[Category: Han, Q.]] | ||
[[Category: Li, J.]] | [[Category: Li, J.]] | ||
| - | [[Category: Robinson, | + | [[Category: Robinson, H.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: KYN]] | [[Category: KYN]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:32:04 2008'' |
Revision as of 16:32, 20 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , and | ||||||
| Ligands: | , and | ||||||
| Gene: | AADAT, KAT2 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of human kynurenine aminotransferase II in complex with kynurenine
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
2R2N is a Single protein structure of sequence from Homo sapiens. 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 Mar 20 18:32:04 2008
