Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin

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...

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Main Authors: Rajan, Sreekanth, Prakash, Ajit, Shin, Joon, Yoon, Ho Sup
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2018
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Online Access:https://hdl.handle.net/10356/88977
http://hdl.handle.net/10220/46041
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-889772023-02-28T17:00:48Z Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin Rajan, Sreekanth Prakash, Ajit Shin, Joon Yoon, Ho Sup School of Biological Sciences FK506-binding domain (FKBD) Nucleic Acid DRNTU::Science::Biological sciences 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. MOE (Min. of Education, S’pore) NMRC (Natl Medical Research Council, S’pore) Published version 2018-09-19T08:37:58Z 2019-12-06T17:15:05Z 2018-09-19T08:37:58Z 2019-12-06T17:15:05Z 2016 Journal Article 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 0305-1048 https://hdl.handle.net/10356/88977 http://hdl.handle.net/10220/46041 10.1093/nar/gkw001 26762975 en Nucleic Acids Research © 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. 17 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic FK506-binding domain (FKBD)
Nucleic Acid
DRNTU::Science::Biological sciences
spellingShingle FK506-binding domain (FKBD)
Nucleic Acid
DRNTU::Science::Biological sciences
Rajan, Sreekanth
Prakash, Ajit
Shin, Joon
Yoon, Ho Sup
Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Rajan, Sreekanth
Prakash, Ajit
Shin, Joon
Yoon, Ho Sup
format Article
author Rajan, Sreekanth
Prakash, Ajit
Shin, Joon
Yoon, Ho Sup
author_sort Rajan, Sreekanth
title Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
title_short Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
title_full Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
title_fullStr Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
title_full_unstemmed Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
title_sort structural basis of nucleic acid recognition by fk506-binding protein 25 (fkbp25), a nuclear immunophilin
publishDate 2018
url https://hdl.handle.net/10356/88977
http://hdl.handle.net/10220/46041
_version_ 1759853168025403392