Mutations within the predicted fragment-binding region of FAM83G/SACK1G abolish its interaction with the Ser/Thr kinase CK1α.

Abstract excerpt

SACK1G (aka FAM83G, PAWS1) plays a central role in activating canonical WNT signalling through interaction with the Ser/Thr kinase CK1α. The loss of CK1α binding and WNT signalling underlies the pathogenesis of palmoplantar keratoderma (PPK) caused by several reported mutations in the SACK1G gene. We modelled the scaffold anchor of CK1 (SACK1) domain of SACK1G and used fragment-bound structures of the SACK1B...

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• Binding Sites
• DLD gene
• Models, Molecular
• Mutation
• Protein Binding