We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2vgz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2vgz.jpg|left|200px]]<br /><applet load="2vgz" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2vgz.jpg|left|200px]]
-
caption="2vgz, resolution 2.30&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II'''<br />
+
{{Structure
 +
|PDB= 2vgz |SIZE=350|CAPTION= <scene name='initialview01'>2vgz</scene>, resolution 2.30&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Iod+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2VGZ 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=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Iod+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGZ OCA].
+
2VGZ 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=2VGZ OCA].
==Reference==
==Reference==
-
Crystal Structure of Human Kynurenine Aminotransferase II, a Drug Target for the Treatment of Schizophrenia., Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M, J Biol Chem. 2008 Feb 8;283(6):3559-66. Epub 2007 Dec 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18056996 18056996]
+
Crystal Structure of Human Kynurenine Aminotransferase II, a Drug Target for the Treatment of Schizophrenia., Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M, J Biol Chem. 2008 Feb 8;283(6):3559-66. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18056996 18056996]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 29: Line 38:
[[Category: transit peptide]]
[[Category: transit peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:55 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:46:28 2008''

Revision as of 16:46, 20 March 2008


PDB ID 2vgz

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II


Overview

Kynurenic acid is an endogenous neuroactive compound whose unbalancing is involved in the pathogenesis and progression of several neurological diseases. Kynurenic acid synthesis in the human brain is sustained by the catalytic activity of two kynurenine aminotransferases, hKAT I and hKAT II. A wealth of pharmacological data highlight hKAT II as a sensible target for the treatment of neuropathological conditions characterized by a kynurenic acid excess, such as schizophrenia and cognitive impairment. We have solved the structure of human KAT II by means of the single-wavelength anomalous dispersion method at 2.3-A resolution. Although closely resembling the classical aminotransferase fold, the hKAT II architecture displays unique features. Structural comparison with a prototypical aspartate aminotransferase reveals a novel antiparallel strand-loop-strand motif that forms an unprecedented intersubunit beta-sheet in the functional hKAT II dimer. Moreover, the N-terminal regions of hKAT II and aspartate aminotransferase appear to have converged to highly similar although 2-fold symmetry-related conformations, which fulfill the same functional role. A detailed structural comparison of hKAT I and hKAT II reveals a larger and more aliphatic character to the active site of hKAT II due to the absence of the aromatic cage involved in ligand binding in hKAT I. The observed structural differences could be exploited for the rational design of highly selective hKAT II inhibitors.

About this Structure

2VGZ 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, a Drug Target for the Treatment of Schizophrenia., Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M, J Biol Chem. 2008 Feb 8;283(6):3559-66. Epub 2007 Dec 5. PMID:18056996

Page seeded by OCA on Thu Mar 20 18:46:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools