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.


1sd1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sd1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sd1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sd1| PDB=1sd1 | SCENE= }}
{{STRUCTURE_1sd1| PDB=1sd1 | SCENE= }}
-
'''STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH FORMYCIN A'''
+
===STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH FORMYCIN A===
-
==Overview==
+
<!--
-
The development of new and effective antiprotozoal drugs has been a difficult challenge because of the close similarity of the metabolic pathways between microbial and mammalian systems. 5'-Methylthioadenosine/S-adenosylhomocysteine (MTA/AdoHcy) nucleosidase is thought to be an ideal target for therapeutic drug design as the enzyme is present in many microbes but not in mammals. MTA/AdoHcy nucleosidase (MTAN) irreversibly depurinates MTA or AdoHcy to form adenine and the corresponding thioribose. The inhibition of MTAN leads to a buildup of toxic byproducts that affect various microbial pathways such as quorum sensing, biological methylation, polyamine biosynthesis, and methionine recycling. The design of nucleosidase-specific inhibitors is complicated by its structural similarity to the human MTA phosphorylase (MTAP). The crystal structures of human MTAP complexed with formycin A and 5'-methylthiotubercidin have been solved to 2.0 and 2.1 A resolution, respectively. Comparisons of the MTAP and MTAN inhibitor complexes reveal size and electrostatic potential differences in the purine, ribose, and 5'-alkylthio binding sites, which account for the substrate specificity and reactions catalyzed. In addition, the differences between the two enzymes have allowed the identification of exploitable regions that can be targeted for the development of high-affinity nucleosidase-specific inhibitors. Sequence alignments of Escherichia coli MTAN, human MTAP, and plant MTA nucleosidases also reveal potential structural changes to the 5'-alkylthio binding site that account for the substrate preference of plant MTA nucleosidases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15122881}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15122881 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15122881}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Purine nucleoside phosphorylase]]
[[Category: Purine nucleoside phosphorylase]]
[[Category: Purine salvage,formycin some]]
[[Category: Purine salvage,formycin some]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:33:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:26:00 2008''

Revision as of 14:26, 28 July 2008

Image:1sd1.png

Template:STRUCTURE 1sd1

STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH FORMYCIN A

Template:ABSTRACT PUBMED 15122881

About this Structure

1SD1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design., Lee JE, Settembre EC, Cornell KA, Riscoe MK, Sufrin JR, Ealick SE, Howell PL, Biochemistry. 2004 May 11;43(18):5159-69. PMID:15122881

Page seeded by OCA on Mon Jul 28 17:26:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sd1"
Personal tools