From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1xse.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1xse.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1xse| PDB=1xse | SCENE= }} | | {{STRUCTURE_1xse| PDB=1xse | SCENE= }} |
| | | | |
| - | '''Crystal Structure of Guinea Pig 11beta-Hydroxysteroid Dehydrogenase Type 1'''
| + | ===Crystal Structure of Guinea Pig 11beta-Hydroxysteroid Dehydrogenase Type 1=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The metabolic reduction of 11-keto groups in glucocorticoid steroids such as cortisone leads to the nuclear receptor ligand cortisol. This conversion is an example of pre-receptor regulation and constitutes a novel pharmacological target for the treatment of metabolic disorders such as insulin resistance and possibly other derangements observed in the metabolic syndrome, such as hyperlipidemia, hypertension, and lowered insulin secretion. This reaction is carried out by the NADPH-dependent type 1 11beta-hydroxysteroid dehydrogenase (11beta-HSD1), an enzyme attached through an integral N-terminal transmembrane helix to the lipid bilayer and located with its active site within the lumen of the endoplasmic reticulum. Here we report the crystal structure of recombinant guinea pig 11beta-HSD1. This variant was determined in complex with NADP at 2.5 A resolution and crystallized in the presence of detergent and guanidinium hydrochloride. The overall structure of guinea pig 11beta-HSD1 shows a clear relationship to other members of the superfamily of short-chain dehydrogenases/reductases but harbors a unique C-terminal helical segment that fulfills three essential functions and accordingly is involved in subunit interactions, contributes to active site architecture, and is necessary for lipid-membrane interactions. The structure provides a model for enzyme-lipid bilayer interactions and suggests a funneling of lipophilic substrates such as steroid hormones from the hydrophobic membrane environment to the enzyme active site. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15542590}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15542590 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15542590}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Svensson, S.]] | | [[Category: Svensson, S.]] |
| | [[Category: 11beta-hydroxysteroid dehydrogenase dimer]] | | [[Category: 11beta-hydroxysteroid dehydrogenase dimer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:27:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:57:56 2008'' |
Revision as of 10:58, 29 July 2008
Template:STRUCTURE 1xse
Crystal Structure of Guinea Pig 11beta-Hydroxysteroid Dehydrogenase Type 1
Template:ABSTRACT PUBMED 15542590
About this Structure
1XSE is a Single protein structure of sequence from Cavia porcellus. Full crystallographic information is available from OCA.
Reference
The crystal structure of guinea pig 11beta-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions., Ogg D, Elleby B, Norstrom C, Stefansson K, Abrahmsen L, Oppermann U, Svensson S, J Biol Chem. 2005 Feb 4;280(5):3789-94. Epub 2004 Nov 12. PMID:15542590
Page seeded by OCA on Tue Jul 29 13:57:56 2008
