메뉴 건너뛰기




Volumn 420, Issue 6916, 2002, Pages 696-700

Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CRYSTAL STRUCTURE; POLYPEPTIDES;

EID: 0037069667     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01268     Document Type: Article
Times cited : (291)

References (30)
  • 5
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. & Hakoshima, T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19, 4449-4462 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 6
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K. M., Lemmon, M. A., Schlessinger, J. & Sigler, P. B. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046 (1995).
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 7
    • 0029096888 scopus 로고
    • Structure of the binding site for inositol phosphates in a PH domain
    • Hyvonen, M. et al. Structure of the binding site for inositol phosphates in a PH domain. EMBO J. 14, 4676-4685 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4676-4685
    • Hyvonen, M.1
  • 8
    • 0033587574 scopus 로고    scopus 로고
    • 2+ inducer, at the D-myo-inositol 1,4,5-trisphosphate receptor
    • 2+ inducer, at the D-myo-inositol 1,4,5-trisphosphate receptor. Biochemistry 38, 9234-9241 (1999).
    • (1999) Biochemistry , vol.38 , pp. 9234-9241
    • Hotoda, H.1
  • 9
    • 0026556882 scopus 로고
    • beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors
    • Murzin, A. G., Lesk, A. M. & Chothia, C. beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors. J. Mol. Biol. 223, 531-543 (1992).
    • (1992) J. Mol. Biol. , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 10
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 11
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of β-catenin
    • Huber, A. H., Nelson, W. J. & Weis, W. I. Three-dimensional structure of the armadillo repeat region of β-catenin. Cell 90, 871-882 (1997).
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 12
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • Cingolani, G., Petosa, C.,Weis, K. & Muller, C. W. Structure of importin-β bound to the IBB domain of importin-α. Nature 399, 221-229 (1999).
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 13
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer, M., Berg, S. & Reynolds, A. B. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 76, 789-791 (1994).
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 14
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure prediction
    • Rost, B., Sander, C. & Schneider, R. PHD - an automatic mail server for protein secondary structure prediction. Comput. Appl. Biosci. 10, 53-60 (1994).
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 15
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones, D. T. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 287, 797-815 (1999).
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 16
    • 0037077304 scopus 로고    scopus 로고
    • Two-state conformational changes in inositol 1,4,5-trisphosphate receptor regulated by calcium
    • Hamada, K., Miyata, T., Mayanagi, K., Hirota, J. & Mikoshiba, K. Two-state conformational changes in inositol 1,4,5-trisphosphate receptor regulated by calcium. J. Biol. Chem. 277, 21115-21118 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 21115-21118
    • Hamada, K.1    Miyata, T.2    Mayanagi, K.3    Hirota, J.4    Mikoshiba, K.5
  • 17
    • 0037099206 scopus 로고    scopus 로고
    • Three-dimensional structure of the type I inositol 1,4,5-trisphosphate receptor at 24 Å resolution
    • Jiang, Q. X., Thrower, E. C., Chester, D. W., Ehrlich, B. E. & Sigworth, F. J. Three-dimensional structure of the type I inositol 1,4,5-trisphosphate receptor at 24 Å resolution. EMBO J. 21, 3575-3581 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3575-3581
    • Jiang, Q.X.1    Thrower, E.C.2    Chester, D.W.3    Ehrlich, B.E.4    Sigworth, F.J.5
  • 18
    • 0031728001 scopus 로고    scopus 로고
    • New developments in the molecular pharmacology of the myo-inositol 1,4,5-trisphosphate receptor
    • Wilcox, R. A., Primrose, W. U. Nahorski, S. R. & Challiss, R. A. New developments in the molecular pharmacology of the myo-inositol 1,4,5-trisphosphate receptor. Trends Pharmacol. Sci. 19, 467-475 (1998).
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 467-475
    • Wilcox, R.A.1    Primrose, W.U.2    Nahorski, S.R.3    Challiss, R.A.4
  • 19
    • 0027190892 scopus 로고
    • Synthesis of 1D-3-deoxy-, 1D-2,3-dideoxy-, and 1D-2,3,6-trideoxy-myo-inositol 1,4,5-trisphosphate from qaebrachitol, their binding affinities, and calcium release activity
    • Kozikowski, A. P., Ognyanov, V. I., Fauq, A. H., Nahorski, A. R. & Wilcox, R. A. Synthesis of 1D-3-deoxy-, 1D-2,3-dideoxy-, and 1D-2,3,6-trideoxy-myo-inositol 1,4,5-trisphosphate from qaebrachitol, their binding affinities, and calcium release activity. J. Am. Chem. Soc. 115, 4429-4434 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4429-4434
    • Kozikowski, A.P.1    Ognyanov, V.I.2    Fauq, A.H.3    Nahorski, A.R.4    Wilcox, R.A.5
  • 20
    • 0029898559 scopus 로고    scopus 로고
    • Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor
    • Yoshikawa, F. et al. Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor. J. Biol. Chem. 271, 18277-18284 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 18277-18284
    • Yoshikawa, F.1
  • 21
    • 0030610150 scopus 로고    scopus 로고
    • 2+ safeguards against spontaneous activity
    • 2+ safeguards against spontaneous activity. Curr. Biol. 7, 510-519 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 510-519
    • Marchant, J.S.1    Taylor, C.W.2
  • 22
    • 0030771866 scopus 로고    scopus 로고
    • 2+-binding domains in the type 1 inositol 1,4,5-trisphosphate receptor
    • 2+-binding domains in the type 1 inositol 1,4,5-trisphosphate receptor. J. Biol. Chem. 272, 25899-25906 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 25899-25906
    • Sienaert, I.1
  • 23
    • 0036646104 scopus 로고    scopus 로고
    • Localization and function of a calmodulin/apocalmodulin binding domain in the N-terminal part of the type 1 inositol 1,4,5-trisphosphate receptor
    • Sienaert, I. et al. Localization and function of a calmodulin/apocalmodulin binding domain in the N-terminal part of the type 1 inositol 1,4,5-trisphosphate receptor. Biochem. J. 365, 269-277 (2002).
    • (2002) Biochem. J. , vol.365 , pp. 269-277
    • Sienaert, I.1
  • 24
    • 0033590930 scopus 로고    scopus 로고
    • High efficient expression of the functional ligand binding site of the inositol 1,4,5-triphosphate receptor in Escherichia coli
    • Yoshikawa, F. et al. High efficient expression of the functional ligand binding site of the inositol 1,4,5-triphosphate receptor in Escherichia coli. Biochem. Biophys. Res Commun. 257, 792-797 (1999).
    • (1999) Biochem. Biophys. Res Commun. , vol.257 , pp. 792-797
    • Yoshikawa, F.1
  • 25
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP- 12 complexes with FK506 and rapamycin
    • Van Duyne, G. D., Standaert, R. E., Karplus, P. A., Schreiber, S. L. & Clardy, J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.E.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 26
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. The finer things in X-ray diffraction data collection. Acta Crystallogr. D 55, 1718-1725 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 27
    • 80055004570 scopus 로고
    • Generalized method of determining heavy-atom positions using the difference Patterson function
    • Terwillinger, T. C., Kim, S. H. & Eisenberg, I. Generalized method of determining heavy-atom positions using the difference Patterson function. Acta Crystallogr A 43, 1-5 (1987).
    • (1987) Acta Crystallogr A , vol.43 , pp. 1-5
    • Terwillinger, T.C.1    Kim, S.H.2    Eisenberg, J.3
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods
    • La Fortelle, E. D. & Bricogne, G. Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • La Fortelle, E.D.1    Bricogne, G.2
  • 29
    • 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 Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 30
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.