메뉴 건너뛰기




Volumn 583, Issue 2, 2009, Pages 320-324

Atomic structure of mutant PPARγ LBD complexed with 15d-PGJ2: Novel modulation mechanism of PPARγ/RXRα function by covalently bound ligands

Author keywords

activating process; covalently bound ligand; Crystal structure; modulation mechanism; PPAR ; PPAR RXR

Indexed keywords

15 DEOXY DELTA12,14 PROSTAGLANDIN J2; CELL NUCLEUS RECEPTOR; CYSTEINE; HETERODIMER; MUTANT PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RETINOID X RECEPTOR ALPHA;

EID: 58249099266     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.12.017     Document Type: Article
Times cited : (42)

References (26)
  • 1
    • 0036189407 scopus 로고    scopus 로고
    • PPARadigms and PPARadoxes: expanding roles for PPARγ in the control of lipid metabolism
    • Walczak R., and Tontonoz P. PPARadigms and PPARadoxes: expanding roles for PPARγ in the control of lipid metabolism. J. Lipid Res. 43 (2002) 177-186
    • (2002) J. Lipid Res. , vol.43 , pp. 177-186
    • Walczak, R.1    Tontonoz, P.2
  • 2
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf D.J., and Evans R.M. The RXR heterodimers and orphan receptors. Cell 83 (1995) 841-850
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 3
    • 0035851187 scopus 로고    scopus 로고
    • PPARγ: a nuclear regulator of metabolism, differentiation, and cell growth
    • Rosen E.D., and Spiegelman B.M. PPARγ: a nuclear regulator of metabolism, differentiation, and cell growth. J. Biol. Chem. 276 (2001) 37731-37734
    • (2001) J. Biol. Chem. , vol.276 , pp. 37731-37734
    • Rosen, E.D.1    Spiegelman, B.M.2
  • 4
    • 0037900979 scopus 로고    scopus 로고
    • Minireview: lipid metabolism, metabolic disease, and peroxisome proliferator-activated receptors
    • Lee C.-H., Olson P., and Evans R.M. Minireview: lipid metabolism, metabolic disease, and peroxisome proliferator-activated receptors. Endocrinology 144 (2003) 2201-2207
    • (2003) Endocrinology , vol.144 , pp. 2201-2207
    • Lee, C.-H.1    Olson, P.2    Evans, R.M.3
  • 5
    • 0034923501 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor γ and metabolic disease
    • Willson T.M., Lambert M.H., and Kliewer S.A. Peroxisome proliferator-activated receptor γ and metabolic disease. Annu. Rev. Biochem. 70 (2001) 341-367
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 341-367
    • Willson, T.M.1    Lambert, M.H.2    Kliewer, S.A.3
  • 6
    • 5344266704 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor γ: its role in metabolic syndrome
    • Pakala R., et al. Peroxisome proliferator-activated receptor γ: its role in metabolic syndrome. Cardiovasc. Radiat. Med. 5 (2004) 97-103
    • (2004) Cardiovasc. Radiat. Med. , vol.5 , pp. 97-103
    • Pakala, R.1
  • 8
    • 0033617520 scopus 로고    scopus 로고
    • Orphan nuclear receptors: shifting endocrinology into reverse
    • Kliewer S.A., Lehmann J.M., and Willson T.M. Orphan nuclear receptors: shifting endocrinology into reverse. Science 284 (1999) 757-760
    • (1999) Science , vol.284 , pp. 757-760
    • Kliewer, S.A.1    Lehmann, J.M.2    Willson, T.M.3
  • 9
    • 29644433449 scopus 로고    scopus 로고
    • Fatty acid transduction of nitric oxide signaling: multiple nitrated unsaturated fatty acid derivatives exist in human blood and urine and serve as endogenous peroxisome proliferator-activated receptor ligands
    • Baker P.R.S., et al. Fatty acid transduction of nitric oxide signaling: multiple nitrated unsaturated fatty acid derivatives exist in human blood and urine and serve as endogenous peroxisome proliferator-activated receptor ligands. J. Biol. Chem. 280 (2005) 42464-42475
    • (2005) J. Biol. Chem. , vol.280 , pp. 42464-42475
    • Baker, P.R.S.1
  • 10
    • 14044275170 scopus 로고    scopus 로고
    • Nitrolinoleic acid: an endogenous peroxisome proliferator-activated receptor γ ligand
    • Schopfer F.J., et al. Nitrolinoleic acid: an endogenous peroxisome proliferator-activated receptor γ ligand. Proc. Natl. Acad. Sci. USA 102 (2005) 2340-2345
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2340-2345
    • Schopfer, F.J.1
  • 11
    • 49449087925 scopus 로고    scopus 로고
    • Molecular recognition of nitrated fatty acids by PPARγ
    • Li Y., et al. Molecular recognition of nitrated fatty acids by PPARγ. Nat. Struct. Mol. Biol. 15 (2008) 865-867
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 865-867
    • Li, Y.1
  • 12
    • 0028972025 scopus 로고
    • 2 is a ligand for the adipocyte determination factor PPARγ
    • 2 is a ligand for the adipocyte determination factor PPARγ. Cell 83 (1995) 803-812
    • (1995) Cell , vol.83 , pp. 803-812
    • Forman, B.M.1
  • 13
    • 0028972026 scopus 로고
    • 2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation
    • 2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation. Cell 83 (1995) 813-819
    • (1995) Cell , vol.83 , pp. 813-819
    • Kliewer, S.A.1
  • 14
    • 51349100657 scopus 로고    scopus 로고
    • Structural basis for the activation of PPARγ by oxidized fatty acids
    • Itoh T., et al. Structural basis for the activation of PPARγ by oxidized fatty acids. Nat. Struct. Mol. Biol. 15 (2008) 924-931
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 924-931
    • Itoh, T.1
  • 15
    • 17144381253 scopus 로고    scopus 로고
    • α, β-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor γ
    • Shiraki T., et al. α, β-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor γ. J. Biol. Chem. 280 (2005) 14145-14153
    • (2005) J. Biol. Chem. , vol.280 , pp. 14145-14153
    • Shiraki, T.1
  • 16
    • 57849098033 scopus 로고    scopus 로고
    • Waku, T. et al. (2008) Structural insight into PPARγ activation through covalent modification with endogenous fatty acids. J. Mol. Biol., doi:10.1016/j.jmb.2008.10.039.
    • Waku, T. et al. (2008) Structural insight into PPARγ activation through covalent modification with endogenous fatty acids. J. Mol. Biol., doi:10.1016/j.jmb.2008.10.039.
  • 17
    • 56749130032 scopus 로고    scopus 로고
    • Structural of the intact PPAR-γ-RXR-α nuclear receptor complex on DNA
    • Chandra V., et al. Structural of the intact PPAR-γ-RXR-α nuclear receptor complex on DNA. Nature 456 (2008) 350-356
    • (2008) Nature , vol.456 , pp. 350-356
    • Chandra, V.1
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol. 276 (1997) 307-326
    • (1997) Method Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: a new software suite for macromolecular structure determination
    • Brunger A.T., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Cryst. D 54 (1998) 905-921
    • (1998) Acta Cryst. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T., et al. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A. 47 (1991) 110-119
    • (1991) Acta Cryst. A. , vol.47 , pp. 110-119
    • Jones, T.1
  • 21
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - a visualization system for exploratory research and analysis
    • Pettersen E., et al. UCSF Chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004) 1605-1612
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.1
  • 22
    • 31544450241 scopus 로고    scopus 로고
    • 2 to the PPARγ ligand-binding domain by multi-wavelength global fitting
    • 2 to the PPARγ ligand-binding domain by multi-wavelength global fitting. Biochem. J. 393 (2006) 749-755
    • (2006) Biochem. J. , vol.393 , pp. 749-755
    • Shiraki, T.1
  • 23
    • 0035923672 scopus 로고    scopus 로고
    • Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors
    • Xu H.E., et al. Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc. Natl. Acad. Sci. USA 98 (2001) 13919-13924
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13919-13924
    • Xu, H.E.1
  • 24
    • 0032505096 scopus 로고    scopus 로고
    • Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ
    • Nolte R.T., et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature 395 (1998) 137-143
    • (1998) Nature , vol.395 , pp. 137-143
    • Nolte, R.T.1
  • 25
    • 0033681001 scopus 로고    scopus 로고
    • Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors
    • Gampe Jr., et al. Asymmetry in the PPARγ/RXRα crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol. Cell 5 (2000) 545-555
    • (2000) Mol. Cell , vol.5 , pp. 545-555
    • Gampe, Jr.1
  • 26
    • 11344266115 scopus 로고    scopus 로고
    • Rational discovery of a novel interface for a coactivator in the peroxisome proliferator-activated receptor γ: Theoretical implications of impairment in type 2 diabetes mellitus
    • Shiraki T., et al. Rational discovery of a novel interface for a coactivator in the peroxisome proliferator-activated receptor γ: Theoretical implications of impairment in type 2 diabetes mellitus. Proteins 58 (2005) 418-425
    • (2005) Proteins , vol.58 , pp. 418-425
    • Shiraki, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.