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Mutation in a flexible linker modulates binding affinity for modular complexes.

Philippa H Stokes¹, Neil O Robertson¹, Ana P G Silva¹

¹School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales, Australia.

|February 22, 2019

Summary

This summary is machine-generated.

Altering the spacer region in tandem beta zippers, like the LHX4-ISL2 complex, impacts binding affinity by increasing linker flexibility, not altering complex structure. This finding is crucial for understanding protein-protein interactions.

Keywords:

intrinsically disordered region modular binding mutation protein complex protein-protein interaction

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Area of Science:

Protein structure and dynamics
Molecular biology
Biochemistry

Background:

Tandem beta zippers are protein complexes formed by linear motifs and partner protein domains.
These complexes involve intrinsically disordered proteins and reveal flexible spacer regions between motifs.
The role of these spacer regions in binding orientation and affinity is not fully understood.

Purpose of the Study:

To investigate the structural and functional impact of mutations within the spacer region of tandem beta zipper complexes.
To elucidate the role of spacer region flexibility in modulating binding affinity.

Main Methods:

Site-directed mutagenesis was used to alter a solvent-exposed side chain in the spacer region of the LHX4-ISL2 complex.
Structural analysis was performed to assess the impact of the mutation on complex structure.
Binding affinity was measured to determine the functional consequences of the mutation.

Main Results:

Mutation of the solvent-exposed side chain in the LHX4-ISL2 spacer region did not significantly alter the complex's structure.
The mutation led to a decrease in binding affinity between LHX4 and ISL2.
This decrease in affinity was attributed to increased flexibility of the linker region.

Conclusions:

Spacer regions in tandem beta zippers play a critical role in regulating binding affinity.
Flexibility within the spacer region, rather than structural integrity, is a key determinant of binding strength.
These findings provide insights into the molecular mechanisms governing protein-protein interactions in intrinsically disordered protein complexes.