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Proteins ; 87(5): 425-429, 2019 05.
Article in English | MEDLINE | ID: mdl-30788856

ABSTRACT

Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which ß-strands form upon binding. Studies of such complexes, formed by LIM domain proteins and linear motifs in their intrinsically disordered partners, revealed spacer regions between the linear motifs that are relatively flexible but may affect the overall orientation of the binding modules. We demonstrate that mutation of a solvent exposed side chain in the spacer region of an LHX4-ISL2 complex has no significant effect on the structure of the complex, but decreases binding affinity, apparently by increasing flexibility of the linker.


Subject(s)
DNA, Intergenic/ultrastructure , DNA-Binding Proteins/ultrastructure , LIM-Homeodomain Proteins/ultrastructure , Transcription Factors/ultrastructure , Amino Acid Sequence , Animals , Binding Sites/genetics , DNA, Intergenic/chemistry , DNA, Intergenic/genetics , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/genetics , LIM-Homeodomain Proteins/chemistry , LIM-Homeodomain Proteins/genetics , Mice , Models, Molecular , Multiprotein Complexes/chemistry , Multiprotein Complexes/genetics , Multiprotein Complexes/ultrastructure , Mutation/genetics , Protein Binding/genetics , Protein Structure, Secondary , Protein Structure, Tertiary , Sequence Homology, Amino Acid , Transcription Factors/chemistry , Transcription Factors/genetics
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