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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| Format: | Journal Article |
| Language: | English |
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2018
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| Online Access: | https://hdl.handle.net/10356/88977 http://hdl.handle.net/10220/46041 |
| _version_ | 1811677333688418304 |
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| author | Rajan, Sreekanth Prakash, Ajit Shin, Joon Yoon, Ho Sup |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Rajan, Sreekanth Prakash, Ajit Shin, Joon Yoon, Ho Sup |
| author_sort | Rajan, Sreekanth |
| collection | NTU |
| 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. |
| first_indexed | 2024-10-01T02:35:42Z |
| format | Journal Article |
| id | ntu-10356/88977 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T02:35:42Z |
| publishDate | 2018 |
| record_format | dspace |
| spelling | ntu-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 |
| 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 |
| title | 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_short | 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 |
| topic | FK506-binding domain (FKBD) Nucleic Acid DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/88977 http://hdl.handle.net/10220/46041 |
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