Bibliographic Details
| Title: |
Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin |
| 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] |
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| Database: |
Engineering Source |
