The structure of an FF domain from human HYPA/FBP11

Mark Allen; Assaf Friedler; Oliver Schon; Mark Bycroft

doi:10.1016/S0022-2836(02)00968-3

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 journal › Article › peer-review

74 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 language	English
Pages (from-to)	411-416
Number of pages	6
Journal	Journal of Molecular Biology
Volume	323
Issue number	3
DOIs	https://doi.org/10.1016/S0022-2836(02)00968-3
State	Published - 2002
Externally published	Yes

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
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10.1016/S0022-2836(02)00968-3

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title = "The structure of an FF domain from human HYPA/FBP11",

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.",

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AU - Allen, Mark

AU - Friedler, Assaf

AU - Schon, Oliver

AU - Bycroft, Mark

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N2 - 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.

AB - 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.

KW - NMR structure

KW - Phosphopeptide recognition

KW - RNA polymerase II carboxyl-terminal domain

KW - Transcription

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The structure of an FF domain from human HYPA/FBP11

Abstract

Bibliographical note

Keywords

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