Solution structure of LXXLL-related cofactor peptide of orphan nuclear receptor FTZ-F1

Ji Hye Yun, Chul Jin Lee, Jin Won Jung, Weontae Lee

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZPEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZPEP formed α-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZPEP. The solution structure of FTZPEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix.

Original languageEnglish
Pages (from-to)583-588
Number of pages6
JournalBulletin of the Korean Chemical Society
Volume33
Issue number2
DOIs
Publication statusPublished - 2012 Feb 20

Fingerprint

Orphan Nuclear Receptors
Peptides
Conformations
Genes
Polytetrafluoroethylene
Transcription
Nuclear magnetic resonance spectroscopy
Ligands

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

@article{b16d55f6ece2433ca3914c988e89a08b,
title = "Solution structure of LXXLL-related cofactor peptide of orphan nuclear receptor FTZ-F1",
abstract = "Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZPEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZPEP formed α-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZPEP. The solution structure of FTZPEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix.",
author = "Yun, {Ji Hye} and Lee, {Chul Jin} and Jung, {Jin Won} and Weontae Lee",
year = "2012",
month = "2",
day = "20",
doi = "10.5012/bkcs.2012.33.2.583",
language = "English",
volume = "33",
pages = "583--588",
journal = "Bulletin of the Korean Chemical Society",
issn = "0253-2964",
publisher = "Korean Chemical Society",
number = "2",

}

Solution structure of LXXLL-related cofactor peptide of orphan nuclear receptor FTZ-F1. / Yun, Ji Hye; Lee, Chul Jin; Jung, Jin Won; Lee, Weontae.

In: Bulletin of the Korean Chemical Society, Vol. 33, No. 2, 20.02.2012, p. 583-588.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Solution structure of LXXLL-related cofactor peptide of orphan nuclear receptor FTZ-F1

AU - Yun, Ji Hye

AU - Lee, Chul Jin

AU - Jung, Jin Won

AU - Lee, Weontae

PY - 2012/2/20

Y1 - 2012/2/20

N2 - Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZPEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZPEP formed α-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZPEP. The solution structure of FTZPEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix.

AB - Functional interaction between Drosophila orphan receptor FTZ-F1 (NR5A3) and a segmentation gene product fushi tarazu (FTZ) is crucial for regulating genes related to define the identities of alternate segmental regions in the Drosophila embryo. FTZ binding to the ligand-binding domain (LBD) of FTZ-F1 is of essence in activating its transcription process. We determined solution structures of the cofactor peptide (FTZPEP) derived from FTZ by NMR spectroscopy. The cofactor peptide showed a nascent helical conformation in aqueous solution, however, the helicity was increased in the presence of TFE. Furthermore, FTZPEP formed α-helical conformation upon FTZ-F1 binding, which provides a receptor bound structure of FTZPEP. The solution structure of FTZPEP in the presence of FTZ-F1 displays a long stretch of the α-helix with a bend in the middle of helix.

UR - http://www.scopus.com/inward/record.url?scp=84863160974&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84863160974&partnerID=8YFLogxK

U2 - 10.5012/bkcs.2012.33.2.583

DO - 10.5012/bkcs.2012.33.2.583

M3 - Article

VL - 33

SP - 583

EP - 588

JO - Bulletin of the Korean Chemical Society

JF - Bulletin of the Korean Chemical Society

SN - 0253-2964

IS - 2

ER -