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Volumn 116, Issue 3, 2004, Pages 417-429

Structural determinants of allosteric ligand activation in RXR heterodimers

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL NUCLEUS RECEPTOR; DIMER; MUTANT PROTEIN; RECEPTOR PROTEIN; RETINOID X RECEPTOR;

EID: 1642304065     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(04)00119-9     Document Type: Article
Times cited : (286)

References (34)
  • 2
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 375:1995;377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 3
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    • Carter P.J., Winter G., Wilkinson A.J., Fersht A.R. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell. 38:1984;835-840.
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 4
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: Opening the X-files
    • Chawla A., Repa J.J., Evans R.M., Mangelsdorf D.J. Nuclear receptors and lipid physiology. Opening the X-files Science. 294:2001;1866-1870.
    • (2001) Science , vol.294 , pp. 1866-1870
    • Chawla, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 5
    • 0029930872 scopus 로고    scopus 로고
    • Modulation of nuclear receptor interactions by ligands: Kinetic analysis using surface plasmon resonance
    • Cheskis B., Freedman L.P. Modulation of nuclear receptor interactions by ligands. kinetic analysis using surface plasmon resonance Biochemistry. 35:1996;3309-3318.
    • (1996) Biochemistry , vol.35 , pp. 3309-3318
    • Cheskis, B.1    Freedman, L.P.2
  • 8
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
    • Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D. Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand. 9-cis retinoic acid EMBO J. 19:2000;2592-2601.
    • (2000) EMBO J. , vol.19 , pp. 2592-2601
    • Egea, P.F.1    Mitschler, A.2    Rochel, N.3    Ruff, M.4    Chambon, P.5    Moras, D.6
  • 10
    • 0037050017 scopus 로고    scopus 로고
    • Co-regulator recruitment and the mechanism of retinoic acid receptor synergy
    • Germain P., Iyer J., Zechel C., Gronemeyer H. Co-regulator recruitment and the mechanism of retinoic acid receptor synergy. Nature. 415:2002;187-192.
    • (2002) Nature , vol.415 , pp. 187-192
    • Germain, P.1    Iyer, J.2    Zechel, C.3    Gronemeyer, H.4
  • 11
    • 0034710876 scopus 로고    scopus 로고
    • Coupled two-way clustering analysis of gene microarray data
    • Getz G., Levine E., Domany E. Coupled two-way clustering analysis of gene microarray data. Proc. Natl. Acad. Sci. USA. 97:2000;12079-12084.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12079-12084
    • Getz, G.1    Levine, E.2    Domany, E.3
  • 12
    • 0029044946 scopus 로고
    • Activation of mammalian retinoid X receptors by the insect growth regulator methoprene
    • Harmon M.A., Boehm M.F., Heyman R.A., Mangelsdorf D.J. Activation of mammalian retinoid X receptors by the insect growth regulator methoprene. Proc. Natl. Acad. Sci. USA. 92:1995;6157-6160.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6157-6160
    • Harmon, M.A.1    Boehm, M.F.2    Heyman, R.A.3    Mangelsdorf, D.J.4
  • 13
    • 0029805887 scopus 로고    scopus 로고
    • An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha
    • Janowski B.A., Willy P.J., Devi T.R., Falck J.R., Mangelsdorf D.J. An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha. Nature. 383:1996;728-731.
    • (1996) Nature , vol.383 , pp. 728-731
    • Janowski, B.A.1    Willy, P.J.2    Devi, T.R.3    Falck, J.R.4    Mangelsdorf, D.J.5
  • 15
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O., Bourne H.R., Cohen F.E. An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 257:1996;342-358.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 16
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S.W., Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science. 286:1999;295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 21
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf D.J., 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
  • 22
    • 0034784920 scopus 로고    scopus 로고
    • Rhodopsin: Structural basis of molecular physiology
    • Menon S.T., Han M., Sakmar T.P. Rhodopsin. structural basis of molecular physiology Physiol. Rev. 81:2001;1659-1688.
    • (2001) Physiol. Rev. , vol.81 , pp. 1659-1688
    • Menon, S.T.1    Han, M.2    Sakmar, T.P.3
  • 24
    • 0026785388 scopus 로고
    • Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids
    • Schmidt A., Endo N., Rutledge S.J., Vogel R., Shinar D., Rodan G.A. Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids. Mol. Endocrinol. 6:1992;1634-1641.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1634-1641
    • Schmidt, A.1    Endo, N.2    Rutledge, S.J.3    Vogel, R.4    Shinar, D.5    Rodan, G.A.6
  • 25
    • 0031043055 scopus 로고    scopus 로고
    • The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor
    • Schulman I.G., Li C., Schwabe J.W., Evans R.M. The phantom ligand effect. allosteric control of transcription by the retinoid X receptor Genes Dev. 11:1997;299-308.
    • (1997) Genes Dev. , vol.11 , pp. 299-308
    • Schulman, I.G.1    Li, C.2    Schwabe, J.W.3    Evans, R.M.4
  • 26
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel G.M., Lockless S.W., Wall M.A., Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat. Struct. Biol. 10:2003;59-69.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 28
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal w. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0032478824 scopus 로고    scopus 로고
    • Heterodimeric DNA binding by the vitamin D receptor and retinoid X receptors is enhanced by 1,25-dihydroxyvitamin D3 and inhibited by 9-cis-retinoic acid. Evidence for allosteric receptor interactions
    • Thompson P.D., Jurutka P.W., Haussler C.A., Whitfield G.K., Haussler M.R. Heterodimeric DNA binding by the vitamin D receptor and retinoid X receptors is enhanced by 1,25-dihydroxyvitamin D3 and inhibited by 9-cis-retinoic acid. Evidence for allosteric receptor interactions. J. Biol. Chem. 273:1998;8483-8491.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8483-8491
    • Thompson, P.D.1    Jurutka, P.W.2    Haussler, C.A.3    Whitfield, G.K.4    Haussler, M.R.5
  • 30
    • 0026350498 scopus 로고
    • Systematic mutational analyses of protein-protein interfaces
    • Wells J.A. Systematic mutational analyses of protein-protein interfaces. Methods Enzymol. 202:1991;390-411.
    • (1991) Methods Enzymol. , vol.202 , pp. 390-411
    • Wells, J.A.1
  • 32
    • 0031042762 scopus 로고    scopus 로고
    • Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR
    • Willy P.J., Mangelsdorf D.J. Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR. Genes Dev. 11:1997;289-298.
    • (1997) Genes Dev. , vol.11 , pp. 289-298
    • Willy, P.J.1    Mangelsdorf, D.J.2
  • 34
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young M.A., Gonfloni S., Superti-Furga G., Roux B., Kuriyan J. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell. 105:2001;115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.