Fig. 3 | Nature Communications

Fig. 3

From: Structure and evolution of the Fam20 kinases

Fig. 3The alternative text for this image may have been generated using AI.

Evolutionarily conserved dimer formation is required for Fam20C activity. a Fam20C mutants display reduced kinase activity. b The crystal structure of drFam20C reveals a homodimer structure resembling the human Fam20A−Fam20C heterodimer. c Detailed view of the drFam20C homodimer interface. All the residues involved in drFam20C homodimer formation are conserved in human Fam20C (the corresponding residues in human Fam20C are indicated in brackets). d Reexamination of the crystal structures of ceFam20 reveals a homodimer structure present in the crystal lattices of two different crystal forms (PDB entries 4KQA and 4KQB). Phe260 and Pro263 are highlighted. e The kinase activity of ceFam20-F260A/P263G is diminished

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