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.


1dyr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dyr.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dyr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dyr| PDB=1dyr | SCENE= }}
{{STRUCTURE_1dyr| PDB=1dyr | SCENE= }}
-
'''THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION'''
+
===THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
BACKGROUND: The fungal pathogen Pneumocystis carinii causes a pneumonia which is an opportunistic infection of AIDS patients. Current therapy includes the dihydrofolate reductase (DHFR) inhibitor trimethoprim which is selective but only a relatively weak inhibitor of the enzyme for P. carinii. Determination of the three-dimensional structure of the enzyme should form the basis for design of more potent and selective therapeutic agents for treatment of the disease. RESULTS: The structure of P. carinii DHFR in complex with reduced nicotinamide adenine dinucleotide phosphate and trimethoprim has accordingly been solved by X-ray crystallography. The structure of the ternary complex has been refined at 1.86 A resolution (R = 0.181). A similar ternary complex with piritrexim (which is a tighter binding, but less selective inhibitor) has also been solved, as has the binary complex holoenzyme, both at 2.5 A resolution. CONCLUSIONS: These structures show how two drugs interact with a fungal DHFR. A comparison of the three-dimensional structure of this relatively large DHFR with bacterial or mammalian enzyme-inhibitor complexes determined previously highlights some additional secondary structure elements in this particular enzyme species. These comparisons provide further insight into the principles governing DHFR-inhibitor interaction, in which the volume of the active site appears to determine the strength of inhibitor binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7866743}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7866743 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7866743}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Stammers, D K.]]
[[Category: Stammers, D K.]]
[[Category: Oxido-reductase]]
[[Category: Oxido-reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:26:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:49:30 2008''

Revision as of 20:49, 30 June 2008

Template:STRUCTURE 1dyr

THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 7866743

About this Structure

1DYR is a Single protein structure of sequence from Pneumocystis carinii. Full crystallographic information is available from OCA.

Reference

The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution., Champness JN, Achari A, Ballantine SP, Bryant PK, Delves CJ, Stammers DK, Structure. 1994 Oct 15;2(10):915-24. PMID:7866743

Page seeded by OCA on Mon Jun 30 23:49:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools