Unique Ligand Binding Patterns between Estrogen Receptor α and β Revealed by HydrogenβDeuterium Exchange.
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| Title: | Unique Ligand Binding Patterns between Estrogen Receptor α and β Revealed by HydrogenβDeuterium Exchange. |
|---|---|
| Authors: | Dai, Susie Y.1,2, Burris, Thomas P.3,4, Dodge, Jeffrey A.3, Montrose-Rafizadeh, Chahrzad3, Yong Wang3, Pascal, Bruce D.5, Chalmers, Michael J.1,5, Griffin, Patrick R.1,5 pgriffin@scripps.edu |
| Source: | Biochemistry. 10/13/2009, Vol. 48 Issue 40, p9668-9676. 9p. |
| Subjects: | Mass spectrometry, Ligand binding (Biochemistry), Quantum perturbations, Chemical structure, Physical & theoretical chemistry |
| Abstract: | Here we present the use of hydrogen—deuterium exchange (HDX) mass spectrometry in analyzing the estrogen receptor/S ligand binding domain (ERβ LBD) in the absence and presence of a variety of chemical compounds with different binding modes and pharmacological properties. Previously, we reported the use of HDX nsa method for predicting the tissue selectivity of ERrs ligands. HDX profiles of ERα LBD in complex with ligand could differentiate compounds of the same chemotype. In contrast, similar analysis of ERβ LBD showed correlation to the compound chemical structures but little correlation with compound tissue selectivity. The different HDX patterns observed for ERβ LBD when compared to those for ERβ LBD bound to the same chemical compounds serve as an indication that ERβ LBD undergoes a different structural response to the same ligand when compared to ERα LBD. The conformational dynamics revealed by HDX for ERβ LBD together with those for ERα LBD shed light on ER ligand interactions and offer new structural insights. The compound-specific perturbations in HDX kinetics observed for each of the two isoforms should aid the development of subtype-selective ER ligands. [ABSTRACT FROM AUTHOR] |
| Copyright of Biochemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 44742037 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Unique Ligand Binding Patterns between Estrogen Receptor α and β Revealed by HydrogenβDeuterium Exchange. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Dai%2C+Susie+Y%2E%22">Dai, Susie Y.</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Burris%2C+Thomas+P%2E%22">Burris, Thomas P.</searchLink><relatesTo>3,4</relatesTo><br /><searchLink fieldCode="AR" term="%22Dodge%2C+Jeffrey+A%2E%22">Dodge, Jeffrey A.</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Montrose-Rafizadeh%2C+Chahrzad%22">Montrose-Rafizadeh, Chahrzad</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Yong+Wang%22">Yong Wang</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Pascal%2C+Bruce+D%2E%22">Pascal, Bruce D.</searchLink><relatesTo>5</relatesTo><br /><searchLink fieldCode="AR" term="%22Chalmers%2C+Michael+J%2E%22">Chalmers, Michael J.</searchLink><relatesTo>1,5</relatesTo><br /><searchLink fieldCode="AR" term="%22Griffin%2C+Patrick+R%2E%22">Griffin, Patrick R.</searchLink><relatesTo>1,5</relatesTo><i> pgriffin@scripps.edu</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biochemistry%22">Biochemistry</searchLink>. 10/13/2009, Vol. 48 Issue 40, p9668-9676. 9p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Mass+spectrometry%22">Mass spectrometry</searchLink><br /><searchLink fieldCode="DE" term="%22Ligand+binding+%28Biochemistry%29%22">Ligand binding (Biochemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Quantum+perturbations%22">Quantum perturbations</searchLink><br /><searchLink fieldCode="DE" term="%22Chemical+structure%22">Chemical structure</searchLink><br /><searchLink fieldCode="DE" term="%22Physical+%26+theoretical+chemistry%22">Physical & theoretical chemistry</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Here we present the use of hydrogen—deuterium exchange (HDX) mass spectrometry in analyzing the estrogen receptor/S ligand binding domain (ERβ LBD) in the absence and presence of a variety of chemical compounds with different binding modes and pharmacological properties. Previously, we reported the use of HDX nsa method for predicting the tissue selectivity of ERrs ligands. HDX profiles of ERα LBD in complex with ligand could differentiate compounds of the same chemotype. In contrast, similar analysis of ERβ LBD showed correlation to the compound chemical structures but little correlation with compound tissue selectivity. The different HDX patterns observed for ERβ LBD when compared to those for ERβ LBD bound to the same chemical compounds serve as an indication that ERβ LBD undergoes a different structural response to the same ligand when compared to ERα LBD. The conformational dynamics revealed by HDX for ERβ LBD together with those for ERα LBD shed light on ER ligand interactions and offer new structural insights. The compound-specific perturbations in HDX kinetics observed for each of the two isoforms should aid the development of subtype-selective ER ligands. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biochemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1021/bi901149t Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 9 StartPage: 9668 Subjects: – SubjectFull: Mass spectrometry Type: general – SubjectFull: Ligand binding (Biochemistry) Type: general – SubjectFull: Quantum perturbations Type: general – SubjectFull: Chemical structure Type: general – SubjectFull: Physical & theoretical chemistry Type: general Titles: – TitleFull: Unique Ligand Binding Patterns between Estrogen Receptor α and β Revealed by HydrogenβDeuterium Exchange. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Dai, Susie Y. – PersonEntity: Name: NameFull: Burris, Thomas P. – PersonEntity: Name: NameFull: Dodge, Jeffrey A. – PersonEntity: Name: NameFull: Montrose-Rafizadeh, Chahrzad – PersonEntity: Name: NameFull: Yong Wang – PersonEntity: Name: NameFull: Pascal, Bruce D. – PersonEntity: Name: NameFull: Chalmers, Michael J. – PersonEntity: Name: NameFull: Griffin, Patrick R. IsPartOfRelationships: – BibEntity: Dates: – D: 13 M: 10 Text: 10/13/2009 Type: published Y: 2009 Identifiers: – Type: issn-print Value: 00062960 Numbering: – Type: volume Value: 48 – Type: issue Value: 40 Titles: – TitleFull: Biochemistry Type: main |
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