Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin
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| Title: | Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin |
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| Authors: | Mchaourab, Hassane S. hassane.mchaourab@vanderbilt.edu, Kumar, M. Satish1, Koteiche, Hanane A.1 |
| Source: | FEBS Letters. May2007, Vol. 581 Issue 10, p1939-1943. 5p. |
| Subjects: | Developmental biology, Equilibrium, Atmospheric temperature, Biochemistry |
| Abstract: | Abstract: To elucidate the structural and energetic basis of attractive protein interactions in the aging lens, we investigated the binding of destabilized mutants of βB1-crystallin to the lens chaperones, α-crystallins. We show that the mutations enhance the binding affinity to αA- but not αB-crystallin at physiological temperatures. Complex formation disrupts the dimer interface of βB1-crystallin consistent with the binding of a monomer. Binding isotherms obtained at increasing concentrations of βB1-crystallin deviate from a classic binding equilibrium and display cooperative-like behavior. In the context of βB1-crystallin unfolding equilibrium, these characteristics are reflective of the concentration-dependent change in the population of a dimeric intermediate that has low affinity to αA-crystallin. In the lens, where α-crystallin binding sites are not regenerated, this may represent an added mechanism to maintain lens transparency. [Copyright &y& Elsevier] |
| Copyright of FEBS Letters is the property of Wiley-Blackwell 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: 24971380 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Mchaourab%2C+Hassane+S%2E%22">Mchaourab, Hassane S.</searchLink><i> hassane.mchaourab@vanderbilt.edu</i><br /><searchLink fieldCode="AR" term="%22Kumar%2C+M%2E+Satish%22">Kumar, M. Satish</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Koteiche%2C+Hanane+A%2E%22">Koteiche, Hanane A.</searchLink><relatesTo>1</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. May2007, Vol. 581 Issue 10, p1939-1943. 5p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Developmental+biology%22">Developmental biology</searchLink><br /><searchLink fieldCode="DE" term="%22Equilibrium%22">Equilibrium</searchLink><br /><searchLink fieldCode="DE" term="%22Atmospheric+temperature%22">Atmospheric temperature</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemistry%22">Biochemistry</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Abstract: To elucidate the structural and energetic basis of attractive protein interactions in the aging lens, we investigated the binding of destabilized mutants of βB1-crystallin to the lens chaperones, α-crystallins. We show that the mutations enhance the binding affinity to αA- but not αB-crystallin at physiological temperatures. Complex formation disrupts the dimer interface of βB1-crystallin consistent with the binding of a monomer. Binding isotherms obtained at increasing concentrations of βB1-crystallin deviate from a classic binding equilibrium and display cooperative-like behavior. In the context of βB1-crystallin unfolding equilibrium, these characteristics are reflective of the concentration-dependent change in the population of a dimeric intermediate that has low affinity to αA-crystallin. In the lens, where α-crystallin binding sites are not regenerated, this may represent an added mechanism to maintain lens transparency. [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of FEBS Letters is the property of Wiley-Blackwell 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: 10.1016/j.febslet.2007.04.005 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 5 StartPage: 1939 Subjects: – SubjectFull: Developmental biology Type: general – SubjectFull: Equilibrium Type: general – SubjectFull: Atmospheric temperature Type: general – SubjectFull: Biochemistry Type: general Titles: – TitleFull: Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Mchaourab, Hassane S. – PersonEntity: Name: NameFull: Kumar, M. Satish – PersonEntity: Name: NameFull: Koteiche, Hanane A. IsPartOfRelationships: – BibEntity: Dates: – D: 15 M: 05 Text: May2007 Type: published Y: 2007 Identifiers: – Type: issn-print Value: 00145793 Numbering: – Type: volume Value: 581 – Type: issue Value: 10 Titles: – TitleFull: FEBS Letters Type: main |
| ResultId | 1 |
