메뉴 건너뛰기




Volumn 77, Issue 6, 2010, Pages 995-1004

Binding of inositol 1,4,5-trisphosphate (IP3) and adenophostin A to the N-Terminal region of the IP3 receptor: Thermodynamic analysis using fluorescence polarization with a novel IP3 receptor ligand

Author keywords

[No Author keywords available]

Indexed keywords

ADENOPHOSTIN A; CALCIUM CHANNEL; FLUORESCEIN ISOTHIOCYANATE; INOSITOL 1,4,5 TRISPHOSPHATE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; LIGAND; PARTIAL AGONIST;

EID: 77952356661     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.109.062596     Document Type: Article
Times cited : (31)

References (43)
  • 1
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames BN and Dubin DT (1960) The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J Biol Chem 235:769-775.
    • (1960) J Biol Chem , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 2
    • 0242582861 scopus 로고    scopus 로고
    • Free-Energy Calculations of Protein-Ligand Cation-π and Amino-π Interactions: From Vacuum to Proteinlike Environments
    • DOI 10.1021/ja035223e
    • Biot C, Buisine E, and Rooman M (2003) Free-energy calculations of protein-ligand cation-π and amino-π interactions: from vacuum to proteinlike environments. J Am Chem Soc 125:13988-13994. (Pubitemid 37420904)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.46 , pp. 13988-13994
    • Biot, C.1    Buisine, E.2    Rooman, M.3
  • 3
    • 0034675855 scopus 로고    scopus 로고
    • Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors
    • Boehning D and Joseph SK (2000) Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors. EMBO J 19:5450-5459.
    • (2000) EMBO J , vol.19 , pp. 5450-5459
    • Boehning, D.1    Joseph, S.K.2
  • 4
    • 0034571319 scopus 로고    scopus 로고
    • Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy?
    • Borea PA, Dalpiaz A, Varani K, Gilli P, and Gilli G (2000) Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy? Biochem Pharmacol 60:1549-1556.
    • (2000) Biochem Pharmacol , vol.60 , pp. 1549-1556
    • Borea, P.A.1    Dalpiaz, A.2    Varani, K.3    Gilli, P.4    Gilli, G.5
  • 5
    • 0032523119 scopus 로고    scopus 로고
    • Binding thermodynamics at the human neuronal nicotine receptor
    • DOI 10.1016/S0006-2952(97)00578-9, PII S0006295297005789
    • Borea PA, Varani K, Gessi S, Gilli P, and Gilli G (1998) Binding thermodynamics at the human neuronal nicotine receptor. Biochem Pharmacol 55:1189-1197. (Pubitemid 28206707)
    • (1998) Biochemical Pharmacology , vol.55 , Issue.8 , pp. 1189-1197
    • Borea, P.A.1    Varani, K.2    Gessi, S.3    Gilli, P.4    Gilli, G.5
  • 8
    • 12344249857 scopus 로고    scopus 로고
    • Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor
    • Bosanac I, Yamazaki H, Matsu-Ura T, Michikawa T, Mikoshiba K, and Ikura M (2005) Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor. Mol Cell 17:193-203.
    • (2005) Mol Cell , vol.17 , pp. 193-203
    • Bosanac, I.1    Yamazaki, H.2    Matsu-Ura, T.3    Michikawa, T.4    Mikoshiba, K.5    Ikura, M.6
  • 9
    • 0031466986 scopus 로고    scopus 로고
    • 2+
    • Cardy TJ, Traynor D, and Taylor CW (1997) Differential regulation of types-1 and -3 inositol trisphosphate receptors by cytosolic Ca2+. Biochem J 328:785-793. (Pubitemid 28005776)
    • (1997) Biochemical Journal , vol.328 , Issue.3 , pp. 785-793
    • Cardy, T.J.A.1    Traynor, D.2    Taylor, C.W.3
  • 10
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • Chaires JB (2008) Calorimetry and thermodynamics in drug design. Annu Rev Biophys 37:135-151.
    • (2008) Annu Rev Biophys , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 12
    • 0029647432 scopus 로고
    • Fluorescence polarization - A new tool for cell and molecular biology
    • Checovich WJ, Bolger RE, and Burke T (1995) Fluorescence polarization - a new tool for cell and molecular biology. Nature 375:254-256.
    • (1995) Nature , vol.375 , pp. 254-256
    • Checovich, W.J.1    Bolger, R.E.2    Burke, T.3
  • 15
    • 0033936050 scopus 로고    scopus 로고
    • Association of the inositol (1,4,5)-trisphosphate receptor ligand binding site with phosphatidylinositol (4,5)-bisphosphate and Adenophostin a
    • DOI 10.1006/mcbr.2000.0208
    • Glouchankova L, Krishna UM, Potter BV, Falck JR, and Bezprozvanny I (2000) Association of the inositol-(1,4,5) trisphosphate receptor ligand binding site with phosphatidylinositol (4,5)-bisphosphate and adenophostin A. Mol Cell Biol Res Commun 3:153-158. (Pubitemid 30430015)
    • (2000) Molecular Cell Biology Research Communications , vol.3 , Issue.3 , pp. 153-158
    • Glouchankova, L.1    Krishna, U.M.2    Potter, B.V.L.3    Falck, J.R.4    Bezprozvanny, I.5
  • 17
    • 0028934572 scopus 로고
    • Fluorescence anisotropy applied to biomolecular interactions
    • Jameson DM and Sawyer WH (1995) Fluorescence anisotropy applied to biomolecular interactions. Methods Enzymol 246:283-300.
    • (1995) Methods Enzymol , vol.246 , pp. 283-300
    • Jameson, D.M.1    Sawyer, W.H.2
  • 21
    • 0032318864 scopus 로고    scopus 로고
    • Structure-based prediction of binding affinities and molecular design of peptide ligands
    • Luque I and Freire E (1998) Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol 295:100-127.
    • (1998) Methods Enzymol , vol.295 , pp. 100-127
    • Luque, I.1    Freire, E.2
  • 23
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • Meyer EA, Castellano RK, and Diederich F (2003) Interactions with aromatic rings in chemical and biological recognition. Angew Chem Int Ed Engl 42:1210-1250.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 25
    • 0036797835 scopus 로고    scopus 로고
    • Determinants of adenophostin a binding to inositolu trisphosphate receptors
    • DOI 10.1042/BJ20020675
    • Morris SA, Nerou EP, Riley AM, Potter BV, and Taylor CW (2002) Determinants of adenophostin A binding to inositol trisphosphate receptors. Biochem J 367:113-120. (Pubitemid 35176897)
    • (2002) Biochemical Journal , vol.367 , Issue.1 , pp. 113-120
    • Morris, S.A.1    Nerou, E.P.2    Riley, A.M.3    Potter, B.V.L.4    Taylor, C.W.5
  • 27
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: Insights for ligand design
    • Olsson TS, Williams MA, Pitt WR, and Ladbury JE (2008) The thermodynamics of protein-ligand interaction and solvation: insights for ligand design. J Mol Biol 384:1002-1117.
    • (2008) J Mol Biol , vol.384 , pp. 1002-1117
    • Olsson, T.S.1    Williams, M.A.2    Pitt, W.R.3    Ladbury, J.E.4
  • 28
    • 33748224042 scopus 로고
    • Chemistry of inositol lipid mediated cellular signaling
    • Potter BV and Lampe D (1995) Chemistry of inositol lipid mediated cellular signaling. Angew Chem Int Ed Engl 34:1933-1972.
    • (1995) Angew Chem Int Ed Engl , vol.34 , pp. 1933-1972
    • Potter, B.V.1    Lampe, D.2
  • 30
    • 2142805871 scopus 로고    scopus 로고
    • 3 affinity matrix
    • DOI 10.1016/j.bbrc.2004.04.051, PII S0006291X04007685
    • Riley AM, Dozol H, Spiess B, and Potter BV (2004) 2-O-(2-aminoethyl)-myo- inositol 1,4,5-trisphosphate as a novel ligand for conjugation: physicochemical properties and synthesis of a new Ins(1,4,5)P3 affinity matrix. Biochem Biophys Res Commun 318:444-452. (Pubitemid 38553800)
    • (2004) Biochemical and Biophysical Research Communications , vol.318 , Issue.2 , pp. 444-452
    • Riley, A.M.1    Dozol, H.2    Spiess, B.3    Potter, B.V.L.4
  • 33
    • 13644272606 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on cation-π interactions in lectin-ligand complexes: High-affinity galectin-3 inhibitors through fine-tuning of an argininearene interaction
    • Sörme P, Arnoux P, Kahl-Knutsson B, Leffler H, Rini JM, and Nilsson UJ (2005) Structural and thermodynamic studies on cation-π interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an argininearene interaction. J Am Chem Soc 127:1737-1743.
    • (2005) J Am Chem Soc , vol.127 , pp. 1737-1743
    • Sörme, P.1    Arnoux, P.2    Kahl-Knutsson, B.3    Leffler, H.4    Rini, J.M.5    Nilsson, U.J.6
  • 35
    • 41149088842 scopus 로고    scopus 로고
    • 2-Position base-modified analogues of adenophostin a as high-affinity agonists of the D-myoinositol trisphosphate receptor: In vitro evaluation and molecular modeling
    • Sureshan KM, Trusselle M, Tovey SC, Taylor CW, and Potter BV (2008) 2-Position base-modified analogues of adenophostin A as high-affinity agonists of the D-myoinositol trisphosphate receptor: in vitro evaluation and molecular modeling. J Org Chem 73:1682-1692.
    • (2008) J Org Chem , vol.73 , pp. 1682-1692
    • Sureshan, K.M.1    Trusselle, M.2    Tovey, S.C.3    Taylor, C.W.4    Potter, B.V.5
  • 38
    • 0037930840 scopus 로고    scopus 로고
    • Critical regions for activation gating of the inositol 1,4,5-trisphosphate receptor
    • DOI 10.1074/jbc.M300646200
    • Uchida K, Miyauchi H, Furuichi T, Michikawa T, and Mikoshiba K (2003) Critical regions for activation gating of the inositol 1,4,5-trisphosphate receptor. J Biol Chem 278:16551-16560. (Pubitemid 36799516)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16551-16560
    • Uchida, K.1    Miyauchi, H.2    Furuichi, T.3    Michikawa, T.4    Mikoshiba, K.5
  • 39
    • 0034162675 scopus 로고    scopus 로고
    • 2+ and calmodulin differentially modulate myo-inositol 1,4,5-trisphosphate (IP3)-binding to the recombinant ligand-binding domains of the various IP3 receptor isoforms
    • 2+ and calmodulin differentially modulate myo-inositol 1,4,5-trisphosphate (IP3)-binding to the recombinant ligand-binding domains of the various IP3 receptor isoforms. Biochem J 346:275-280.
    • (2000) Biochem J , vol.346 , pp. 275-280
    • Vanlingen, S.1    Sipma, H.2    De Smet, P.3    Callewaert, G.4    Missiaen, L.5    De Smedt, H.6    Parys, J.B.7
  • 40
    • 0018607313 scopus 로고
    • Fundamental difference between the molecular interactions of agonists and antagonists with the β-adrenergic receptor
    • Weiland GA, Minneman KP, and Molinoff PB (1979) Fundamental difference between the molecular interactions of agonists and antagonists with the β-adrenergic receptor. Nature 281:114-117.
    • (1979) Nature , vol.281 , pp. 114-117
    • Weiland, G.A.1    Minneman, K.P.2    Molinoff, P.B.3
  • 41
    • 10944261243 scopus 로고    scopus 로고
    • Understanding noncovalent interactions: Ligand binding energy and catalytic efficiency from ligand-induced reductions in motion within receptors and enzymes
    • Williams DH, Stephens E, O'Brien DP, and Zhou M (2004) Understanding noncovalent interactions: ligand binding energy and catalytic efficiency from ligand-induced reductions in motion within receptors and enzymes. Angew Chem Int Ed Engl 43:6596-6616.
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 6596-6616
    • Williams, D.H.1    Stephens, E.2    O'Brien, D.P.3    Zhou, M.4
  • 43


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.