This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1gw6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gw6.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1gw6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gw6| PDB=1gw6 | SCENE= }}
{{STRUCTURE_1gw6| PDB=1gw6 | SCENE= }}
-
'''STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT'''
+
===STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT===
-
==Overview==
+
<!--
-
Leukotriene A4 (LTA4, 5S-trans-5,6-oxido-7,9-trans-11,14-cis-eicosatetraenoic acid) hydrolase (LTA4H)/aminopeptidase is a bifunctional zinc metalloenzyme that catalyzes the final and rate-limiting step in the biosynthesis of leukotriene B4 (LTB4, 5S,12R-dihydroxy-6,14-cis-8,10-trans-eicosatetraenoic acid), a classical chemoattractant and immune modulating lipid mediator. Two chemical features are key to the bioactivity of LTB4, namely, the chirality of the 12R-hydroxyl group and the cis-trans-trans geometry of the conjugated triene structure. From the crystal structure of LTA4H, a hydrophilic patch composed of Gln-134, Tyr-267, and Asp-375 was identified in a narrow and otherwise hydrophobic pocket, believed to bind LTA4. In addition, Asp-375 belongs to peptide K21, a previously characterized 21-residue active site-peptide to which LTA4 binds during suicide inactivation. In the present report we used site-directed mutagenesis and x-ray crystallography to show that Asp-375, but none of the other candidate residues, is specifically required for the epoxide hydrolase activity of LTA4H. Thus, mutation of Asp-375 leads to a selective loss of the enzyme's ability to generate LTB4 whereas the aminopeptidase activity is preserved. We propose that Asp-375, possibly assisted by Gln-134, acts as a critical determinant for the stereoselective introduction of the 12R-hydroxyl group and thus the biological activity of LTB4.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11917124}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11917124 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11917124}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Mutagenesis study]]
[[Category: Mutagenesis study]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:05:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:12:09 2008''

Revision as of 03:12, 1 July 2008

Image:1gw6.png

Template:STRUCTURE 1gw6

STRUCTURE OF LEUKOTRIENE A4 HYDROLASE D375N MUTANT

Template:ABSTRACT PUBMED 11917124

About this Structure

1GW6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:11917124

Page seeded by OCA on Tue Jul 1 06:12:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gw6"
Personal tools