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.

1w7m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w7m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1w7m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w7m| PDB=1w7m | SCENE= }}
{{STRUCTURE_1w7m| PDB=1w7m | SCENE= }}
-
'''CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE'''
+
===CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE===
-
==Overview==
+
<!--
-
The kynurenine pathway has long been regarded as a valuable target for the treatment of several neurological disorders accompanied by unbalanced levels of metabolites along the catabolic cascade, kynurenic acid among them. The irreversible transamination of kynurenine is the sole source of kynurenic acid, and it is catalyzed by different isoforms of the 5'-pyridoxal phosphate-dependent kynurenine aminotransferase (KAT). The KAT-I isozyme has also been reported to possess beta-lyase activity toward several sulfur- and selenium-conjugated molecules, leading to the proposal of a role of the enzyme in carcinogenesis associated with environmental pollutants. We solved the structure of human KAT-I in its 5'-pyridoxal phosphate and pyridoxamine phosphate forms and in complex with the competing substrate l-Phe. The enzyme active site revealed a striking crown of aromatic residues decorating the ligand binding pocket, which we propose as a major molecular determinant for substrate recognition. Ligand-induced conformational changes affecting Tyr(101) and the Trp(18)-bearing alpha-helix H1 appear to play a central role in catalysis. Our data reveal a key structural role of Glu(27), providing a molecular basis for the reported loss of enzymatic activity displayed by the equivalent Glu --&gt; Gly mutation in KAT-I of spontaneously hypertensive rats.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15364907}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15364907 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15364907}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Pyridoxal phosphate]]
[[Category: Pyridoxal phosphate]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:16:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:17:03 2008''

Revision as of 17:17, 28 July 2008

Image:1w7m.png

Template:STRUCTURE 1w7m

CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE

Template:ABSTRACT PUBMED 15364907

About this Structure

1W7M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human kynurenine aminotransferase I., Rossi F, Han Q, Li J, Li J, Rizzi M, J Biol Chem. 2004 Nov 26;279(48):50214-20. Epub 2004 Sep 10. PMID:15364907

Page seeded by OCA on Mon Jul 28 20:17:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w7m"
Personal tools