Home
Resources
Publications
Crystal Structure of the C-terminal Domain of the RAP74 Subunit of Human Transcription Factor IIF

Crystal Structure of the C-terminal Domain of the RAP74 Subunit of Human Transcription Factor IIF

K Kamada, J De Angelis, R G Roeder, S K Burley

Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3115-20.

PMID: 11248041

Abstract:

The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-A resolution. The alpha/beta structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3gamma (HNF-3gamma), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3gamma and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the beta subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42414918	TFIIF (RAP74 subunit) human			Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: