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  Basic Tilted Helix Bundle – A new protein fold in human FKBP25/FKBP3 and HectD1

Helander, S., Montecchio, M., Lemak, A., Farès, C., Almlöf, J., Li, Y., et al. (2014). Basic Tilted Helix Bundle – A new protein fold in human FKBP25/FKBP3 and HectD1. Biochemical and Biophysical Research Communications, 447(1), 26-31. doi:10.1016/j.bbrc.2014.03.068.

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 Creators:
Helander, Sara1, Author
Montecchio , Meri1, Author
Lemak, Alexander2, 3, Author
Farès, Christophe2, Author           
Almlöf , Jonas1, Author
Li, Yanjun4, Author
Yee, Adelina2, 3, Author
Arrowsmith , Cheryl H.2, 3, 4, Author
Dhe-Paganon, Sirano4, Author
Sunnerhagen, Maria1, Author
Affiliations:
1Department of Physics, Chemistry and Biology, Division of Chemistry, Linköping University, SE-58183 Linköping, Sweden, ou_persistent22              
2Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada, ou_persistent22              
3Northeast Structural Genomics Consortium, Toronto, Ontario, Canada, ou_persistent22              
4Structural Genomics Consortium, University of Toronto, 101 College St, Toronto, Ontario M5G 1L7, Canada, ou_persistent22              

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Free keywords: Immunophillins; NMR structure; Structural genomics; FKBP25; FKBP3; HectD1; YY1
 Abstract: In this paper, we describe the structure of a N-terminal domain motif in nuclear-localized FKBP251–73, a member of the FKBP family, together with the structure of a sequence-related subdomain of the E3 ubiquitin ligase HectD1 that we show belongs to the same fold. This motif adopts a compact 5-helix bundle which we name the Basic Tilted Helix Bundle (BTHB) domain. A positively charged surface patch, structurally centered around the tilted helix H4, is present in both FKBP25 and HectD1 and is conserved in both proteins, suggesting a conserved functional role. We provide detailed comparative analysis of the structures of the two proteins and their sequence similarities, and analysis of the interaction of the proposed FKBP25 binding protein YY1. We suggest that the basic motif in BTHB is involved in the observed DNA binding of FKBP25, and that the function of this domain can be affected by regulatory YY1 binding and/or interactions with adjacent domains.

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Language(s): eng - English
 Dates: 2014-03-112014-03-222014-04-25
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbrc.2014.03.068
 Degree: -

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Title: Biochemical and Biophysical Research Communications
  Other : Biochem. Biophys. Res. Commun.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 447 (1) Sequence Number: - Start / End Page: 26 - 31 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1