Mutagenesis of Inc.

<b>(A)</b> Alignment of Inc and its human orthologs. Identical and similar residues are shaded in black and gray respectively. Locations of Inc truncations and point mutants are indicated by arrowheads and closed circles, respectively. <b>(B)</b> Surface rendering of adjacent BTB domains from the crystal structure of human KCTD5 [<a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1011574#pgen.1011574.ref039" target="_blank">39</a>]. Here and in subsequent figure panels, Inc residue numbers are superimposed on conserved equivalents in KCTD5. Inc residues whose mutation specifically weakens Inc-Cul3 associations are highlighted in magenta; other mutated residues are highlighted in blue. <b>(C)</b> Ribbon rendering of adjacent KCTD5 BTB domains. Side chains are shown for Inc residues mutated to assess Inc multimerization. Note that the T36A/D71A/R85E triple mutant alters both faces of Inc. <b>(D)</b> Surface (left) and ribbon (right) rendering of human KCTD5. Inc C-terminal point mutants are labeled and indicated in magenta; side chains are shown in the ribbon rendering. Note that KCTD5 residues equivalent to Inc amino acids 186–211 are not resolved in the crystal structure, suggesting that they are disordered. (PDF)

Publication Details

Journal
Figshare
Published
2025-01-22
DOI
https://doi.org/10.1371/journal.pgen.1011574.s001
Primary Topic
Wheat and Barley Genetics and Pathology
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article
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article

Mutagenesis of Inc.

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Wheat and Barley Genetics and Pathology
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Mutagenesis of Inc.

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Abstract

<b>(A)</b> Alignment of Inc and its human orthologs. Identical and similar residues are shaded in black and gray respectively. Locations of Inc truncations and point mutants are indicated by arrowheads and closed circles, respectively. <b>(B)</b> Surface rendering of adjacent BTB domains from the crystal structure of human KCTD5 [<a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1011574#pgen.1011574.ref039" target="_blank">39</a>]. Here and in subsequent figure panels, Inc residue numbers are superimposed on conserved equivalents in KCTD5. Inc residues whose mutation specifically weakens Inc-Cul3 associations are highlighted in magenta; other mutated residues are highlighted in blue. <b>(C)</b> Ribbon rendering of adjacent KCTD5 BTB domains. Side chains are shown for Inc residues mutated to assess Inc multimerization. Note that the T36A/D71A/R85E triple mutant alters both faces of Inc. <b>(D)</b> Surface (left) and ribbon (right) rendering of human KCTD5. Inc C-terminal point mutants are labeled and indicated in magenta; side chains are shown in the ribbon rendering. Note that KCTD5 residues equivalent to Inc amino acids 186–211 are not resolved in the crystal structure, suggesting that they are disordered. (PDF)

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Wheat and Barley Genetics and Pathology
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