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. 2002 Oct 25;323(3):411-6.
doi: 10.1016/s0022-2836(02)00968-3.

The structure of an FF domain from human HYPA/FBP11

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The structure of an FF domain from human HYPA/FBP11

Mark Allen et al. J Mol Biol. .

Abstract

The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.

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