Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88977
Title: Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
Authors: Rajan, Sreekanth
Prakash, Ajit
Shin, Joon
Yoon, Ho Sup
Keywords: FK506-binding domain (FKBD)
Nucleic Acid
DRNTU::Science::Biological sciences
Issue Date: 2016
Source: Prakash, A., Shin, J., Rajan, S., & Yoon, H. S. (2016). Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin. Nucleic Acids Research, 44(6), 2909-2925. doi:10.1093/nar/gkw001
Series/Report no.: Nucleic Acids Research
Abstract: The nuclear immunophilin FKBP25 interacts with chromatin-related proteins and transcription factors and is suggested to interact with nucleic acids. Currently the structural basis of nucleic acid binding by FKBP25 is unknown. Here we determined the nuclear magnetic resonance (NMR) solution structure of full-length human FKBP25 and studied its interaction with DNA. The FKBP25 structure revealed that the N-terminal helix-loop-helix (HLH) domain and C-terminal FK506-binding domain (FKBD) interact with each other and that both of the domains are involved in DNA binding. The HLH domain forms major-groove interactions and the basic FKBD loop cooperates to form interactions with an adjacent minor-groove of DNA. The FKBP25–DNA complex model, supported by NMR and mutational studies, provides structural and mechanistic insights into the nuclear immunophilin-mediated nucleic acid recognition.
URI: https://hdl.handle.net/10356/88977
http://hdl.handle.net/10220/46041
ISSN: 0305-1048
DOI: http://dx.doi.org/10.1093/nar/gkw001
Rights: © 2016 The Author(s). Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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