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.


1q5m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q5m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1q5m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q5m| PDB=1q5m | SCENE= }}
{{STRUCTURE_1q5m| PDB=1q5m | SCENE= }}
-
'''Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH'''
+
===Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH===
-
==Overview==
+
<!--
-
The aldo-keto reductase rabbit 20alpha-hydroxysteroid dehydrogenase (rb20alpha-HSD; AKR1C5) is less selective than other HSDs, since it exerts its activity both on androgens (C19 steroids) and progestins (C21 steroids). In order to identify the molecular determinants responsible for this reduced selectivity, binary (NADPH) and ternary (NADP(+)/testosterone) complex structures were solved to 1.32A and 2.08A resolution, respectively. Inspection of the cofactor-binding cavity led to the identification of a new interaction between side-chains of residues His222 and Lys270, which cover the central phosphate chain of the cofactor, reminiscent of the "safety-belt" found in other aldo-keto reductases. Testosterone is stabilized by a phenol/benzene tunnel composed of side-chains of numerous residues, among which Phe54, which forces the steroid to take up an orientation markedly contrasting with that found in HSD ternary complexes reported. Combining structural, site-directed mutagenesis, kinetic and fluorescence titration studies, we found that the selectivity of rb20alpha-HSD is mediated by (i) the relaxation of loop B (residues 223-230), partly controlled by the nature of residue 230, (ii) the nature of the residue found at position 54, and (iii) the residues found in the C-terminal tail of the protein especially the side-chain of the amino acid 306.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15123423}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15123423 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15123423}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hydroxysteroid dehydrogenase]]
[[Category: Hydroxysteroid dehydrogenase]]
[[Category: Nadph]]
[[Category: Nadph]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:53:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:45:16 2008''

Revision as of 03:45, 28 July 2008

Image:1q5m.png

Template:STRUCTURE 1q5m

Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH

Template:ABSTRACT PUBMED 15123423

About this Structure

1Q5M is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Loop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily., Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton R, J Mol Biol. 2004 May 21;339(1):89-102. PMID:15123423

Page seeded by OCA on Mon Jul 28 06:45:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q5m"
Personal tools