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.


1ov4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ov4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ov4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ov4| PDB=1ov4 | SCENE= }}
{{STRUCTURE_1ov4| PDB=1ov4 | SCENE= }}
-
'''Crystal structure of human DHEA-ST complexed with androsterone'''
+
===Crystal structure of human DHEA-ST complexed with androsterone===
-
==Overview==
+
<!--
-
In steroid biosynthesis, human dehydroepiandrosterone sulfotransferase (DHEA-ST) in the adrenals has been reported to catalyze the transfer of the sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate to dehydroepiandrosterone (DHEA). DHEA and its sulfate play roles as steroid precursors; however, the role of the enzyme in the catabolism of androgens is poorly understood. Androsterone sulfate is clinically recognized as one of the major androgen metabolites found in urine. Here it is demonstrated that this enzyme recognizes androsterone (ADT) as a cognate substrate with similar kinetics but a 2-fold specificity and stronger substrate inhibition than DHEA. The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition. Structural analysis has revealed the binding mode of ADT differs from that of DHEA, despite the similarity of the overall structure between the ADT and the DHEA binary complexes. Our results identify that this human enzyme is an ADT sulfotransferase as well as a DHEA sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14573603}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14573603 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14573603}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Shi, R.]]
[[Category: Shi, R.]]
[[Category: Alpha/beta fold]]
[[Category: Alpha/beta fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:18:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:02:35 2008''

Revision as of 09:02, 28 July 2008

Image:1ov4.png

Template:STRUCTURE 1ov4

Crystal structure of human DHEA-ST complexed with androsterone

Template:ABSTRACT PUBMED 14573603

About this Structure

1OV4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex., Chang HJ, Shi R, Rehse P, Lin SX, J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. PMID:14573603

Page seeded by OCA on Mon Jul 28 12:02:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ov4"
Personal tools