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| {{STRUCTURE_1ov4| PDB=1ov4 | SCENE= }} | | {{STRUCTURE_1ov4| PDB=1ov4 | SCENE= }} |
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| '''Crystal structure of human DHEA-ST complexed with androsterone'''
| | ===Crystal structure of human DHEA-ST complexed with androsterone=== |
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| ==Overview==
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| 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. |
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| | {{ABSTRACT_PUBMED_14573603}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[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'' |