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.

1d3g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1d3g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1d3g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1d3g| PDB=1d3g | SCENE= }}
{{STRUCTURE_1d3g| PDB=1d3g | SCENE= }}
-
'''HUMAN DIHYDROOROTATE DEHYDROGENASE COMPLEXED WITH BREQUINAR ANALOG'''
+
===HUMAN DIHYDROOROTATE DEHYDROGENASE COMPLEXED WITH BREQUINAR ANALOG===
-
==Overview==
+
<!--
-
BACKGROUND: Dihydroorotate dehydrogenase (DHODH) catalyzes the fourth committed step in the de novo biosynthesis of pyrimidines. As rapidly proliferating human T cells have an exceptional requirement for de novo pyrimidine biosynthesis, small molecule DHODH inhibitors constitute an attractive therapeutic approach to autoimmune diseases, immunosuppression, and cancer. Neither the structure of human DHODH nor any member of its family was known. RESULTS: The high-resolution crystal structures of human DHODH in complex with two different inhibitors have been solved. The initial set of phases was obtained using multiwavelength anomalous diffraction phasing with selenomethionine-containing DHODH. The structures have been refined to crystallographic R factors of 16.8% and 16.2% at resolutions of 1. 6 A and 1.8 A for inhibitors related to brequinar and leflunomide, respectively. CONCLUSIONS: Human DHODH has two domains: an alpha/beta-barrel domain containing the active site and an alpha-helical domain that forms the opening of a tunnel leading to the active site. Both inhibitors share a common binding site in this tunnel, and differences in the binding region govern drug sensitivity or resistance. The active site of human DHODH is generally similar to that of the previously reported bacterial active site. The greatest differences are that the catalytic base removing the proton from dihydroorotate is a serine rather than a cysteine, and that packing of the flavin mononucleotide in its binding site is tighter.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10673429}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10673429 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10673429}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Protein-antiproliferative agent complex]]
[[Category: Protein-antiproliferative agent complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:24:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:18:29 2008''

Revision as of 19:18, 30 June 2008

Image:1d3g.png

Template:STRUCTURE 1d3g

HUMAN DIHYDROOROTATE DEHYDROGENASE COMPLEXED WITH BREQUINAR ANALOG

Template:ABSTRACT PUBMED 10673429

About this Structure

1D3G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents., Liu S, Neidhardt EA, Grossman TH, Ocain T, Clardy J, Structure. 2000 Jan 15;8(1):25-33. PMID:10673429

Page seeded by OCA on Mon Jun 30 22:18:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d3g"
Personal tools