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

78 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
Transcription

Access to Document

10.1016/S0022-2836(02)00968-3

Cite this

@article{5c36b3538a0c4eaa882f47010cbcb393,

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.",

keywords = "NMR structure, Phosphopeptide recognition, RNA polymerase II carboxyl-terminal domain, Transcription",

author = "Mark Allen and Assaf Friedler and Oliver Schon and Mark Bycroft",

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.",

year = "2002",

doi = "10.1016/S0022-2836(02)00968-3",

language = "אנגלית",

volume = "323",

pages = "411--416",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "3",

}

TY - JOUR

T1 - The structure of an FF domain from human HYPA/FBP11

AU - Allen, Mark

AU - Friedler, Assaf

AU - Schon, Oliver

AU - Bycroft, Mark

N1 - 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.

PY - 2002

Y1 - 2002

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

UR - https://www.scopus.com/pages/publications/0036407694

U2 - 10.1016/S0022-2836(02)00968-3

DO - 10.1016/S0022-2836(02)00968-3

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 12381297

AN - SCOPUS:0036407694

SN - 0022-2836

VL - 323

SP - 411

EP - 416

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -

The structure of an FF domain from human HYPA/FBP11

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Fingerprint

Cite this