Title of article :
The Structure of an FF Domain from Human HYPA/FBP11
Author/Authors :
Mark Allen، نويسنده , , Assaf Friedler، نويسنده , , Oliver Schon، نويسنده , , Mark Bycroft، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2002
Pages :
6
From page :
411
To page :
416
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.
Keywords :
Transcription , NMR structure , phosphopeptide recognition , RNA polymerase II carboxyl-terminal domain
Journal title :
Journal of Molecular Biology
Serial Year :
2002
Journal title :
Journal of Molecular Biology
Record number :
1242104
Link To Document :
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