The structure of an FF domain from human HYPA/FBP11

Mark Allen, Assaf Friedler, Oliver Schon, Mark Bycroft*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

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 α helices arranged in an orthogonal bundle with a 310 helix in the loop between the second and third α helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.

Original languageAmerican English
Pages (from-to)411-416
Number of pages6
JournalJournal of Molecular Biology
Volume323
Issue number3
DOIs
StatePublished - 2002
Externally publishedYes

Bibliographical note

Funding Information:
O.S. is supported by a fellowship from the Friedrich-Ebert-Foundation (GER). A.F. is supported by a long-term fellowship, no. LT00056/2000-M, from the Human Frontier Science Program Organisation.

Keywords

  • NMR structure
  • Phosphopeptide recognition
  • RNA polymerase II carboxyl-terminal domain
  • Transcription

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