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PMID: 12381297 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The structure of an FF domain from human HYPA/FBP11.

Journal of molecular biology ·Vol. 323 ·No. 3 ·2002-10-25 ·Pages 411-6

Allen M, Friedler A, Schon O, Bycroft M

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.

MeSH Terms
Amino Acid Sequence Binding Sites Carrier Proteins/chemistry,genetics,metabolism Humans Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Phosphopeptides/metabolism Protein Binding Protein Conformation Protein Folding Protein Structure, Tertiary Sequence Alignment
Chemicals
Carrier Proteins Phosphopeptides
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Allen Mark
MRC Centre for Protein Engineering, Cambridge, UK.
Friedler Assaf
Schon Oliver
Bycroft Mark
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
2002-10-25
Pages
411-6
Language
English
Region
England
NLM ID
2985088R
Subset
IM
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