| Literature DB >> 12381297 |
Mark Allen1, Assaf Friedler, Oliver Schon, Mark Bycroft.
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.Entities:
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Year: 2002 PMID: 12381297 DOI: 10.1016/s0022-2836(02)00968-3
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469