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Volumn 7, Issue 9, 2000, Pages 808-815

Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor

Author keywords

[No Author keywords available]

Indexed keywords

PROLACTIN; PROLACTIN RECEPTOR;

EID: 0033813066     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/79047     Document Type: Article
Times cited : (79)

References (48)
  • 1
    • 0000977534 scopus 로고
    • Actions of prolactin among the vertebrates
    • (ed., Barrington, E.J.W.), Academic Press, New York
    • DeVlaming, V. Actions of prolactin among the vertebrates. In Hormones and evolution (ed., Barrington, E.J.W.), 561-642 (Academic Press, New York; 1979).
    • (1979) Hormones and Evolution , pp. 561-642
    • Devlaming, V.1
  • 2
    • 0029035666 scopus 로고
    • Structural variants of prolactin: Occurrence and physiological significance
    • Sinha, Y.N. Structural variants of prolactin: occurrence and physiological significance. Endocrine Rev. 16, 354-369 (1995).
    • (1995) Endocrine Rev. , vol.16 , pp. 354-369
    • Sinha, Y.N.1
  • 3
    • 0029825056 scopus 로고    scopus 로고
    • Sequence-function relationships within the expanding family of prolactin, growth hormone, placental lactogen, and related proteins in mammals
    • Goffin, V., Shiverick, K.T., Kelly, P.A. & Martial, J.A. Sequence-function relationships within the expanding family of prolactin, growth hormone, placental lactogen, and related proteins in mammals. Endocrine Rev. 17, 385-410 (1996).
    • (1996) Endocrine Rev. , vol.17 , pp. 385-410
    • Goffin, V.1    Shiverick, K.T.2    Kelly, P.A.3    Martial, J.A.4
  • 4
    • 0022721745 scopus 로고
    • Structural features of prolactins and growth hormones that can be related to their biological properties
    • Nicoll, C.S., Mayer, G.L & Russel, S.M. Structural features of prolactins and growth hormones that can be related to their biological properties. Endocrine Rev. 7, 169-203 (1986).
    • (1986) Endocrine Rev. , vol.7 , pp. 169-203
    • Nicoll, C.S.1    Mayer, G.L.2    Russel, S.M.3
  • 5
    • 0029785849 scopus 로고    scopus 로고
    • Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization
    • Gertler, A., Grosclaude, J., Strasburger, C.J., Nir, S. & Djiane, J. Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization. J. Biol. Chem. 271, 24482-24491 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 24482-24491
    • Gertler, A.1    Grosclaude, J.2    Strasburger, C.J.3    Nir, S.4    Djiane, J.5
  • 6
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos, A.M., Ultsch, M. & Kossiakoff, A.A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312 (1992).
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 7
    • 0026263831 scopus 로고
    • The growth hormone/prolactin receptor gene family
    • Kelly, P.A., et al. The growth hormone/prolactin receptor gene family. Oxford Surveys On Eukaryotic Genes 7, 29-50 (1991).
    • (1991) Oxford Surveys On Eukaryotic Genes , vol.7 , pp. 29-50
    • Kelly, P.A.1
  • 8
    • 0029069145 scopus 로고
    • Transcriptional responses to polypeptide ligands: The JAK-STAT pathway
    • Schindler, C. & Darnell, J.E.J. Transcriptional responses to polypeptide ligands: the JAK-STAT pathway. Annu. Rev. Biochem. 64, 621-651 (1995).
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 621-651
    • Schindler, C.1    Darnell, J.E.J.2
  • 9
    • 0028241548 scopus 로고
    • Signaling by the cytokine receptor superfamily: JAKs and STATs
    • Ihle, J.N., et al. Signaling by the cytokine receptor superfamily: JAKs and STATs. Trends Biochem. Sci. 19, 222-227 (1994).
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 222-227
    • Ihle, J.N.1
  • 10
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J.F Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87, 6934-6938 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 11
    • 0025326350 scopus 로고
    • A new cytokine receptor superfamily
    • Cosman, D., et al. A new cytokine receptor superfamily. Trends Biochem. Sci. 15, 265-270 (1990).
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 265-270
    • Cosman, D.1
  • 12
    • 0026764441 scopus 로고
    • Rational design of potent antagonists to the human growth hormone receptor
    • Fuh, G., et al. Rational design of potent antagonists to the human growth hormone receptor. Science 256, 1677-1680 (1992).
    • (1992) Science , vol.256 , pp. 1677-1680
    • Fuh, G.1
  • 13
    • 0028788490 scopus 로고
    • Preparation and characterization of recombinant prolactin receptor extracellular domain from rat
    • Sandowski, Y., et al. Preparation and characterization of recombinant prolactin receptor extracellular domain from rat. Mol. Cell. Endocrinol. 115, 1-11 (1995).
    • (1995) Mol. Cell. Endocrinol. , vol.115 , pp. 1-11
    • Sandowski, Y.1
  • 14
    • 0028941330 scopus 로고
    • Extracellular domain of prolactin receptor from bovine mammary gland: Expression in Escherichia coli, purification and characterization of its interaction with lactogenic hormones
    • Tchelet, A. Extracellular domain of prolactin receptor from bovine mammary gland: expression in Escherichia coli, purification and characterization of its interaction with lactogenic hormones. J. Endocrinol. 144, 393-403 (1995).
    • (1995) J. Endocrinol. , vol.144 , pp. 393-403
    • Tchelet, A.1
  • 15
    • 0031043215 scopus 로고    scopus 로고
    • Large-scale preparation and characterization of recombinant ovine placental lactogen
    • Sakal, E., et al. Large-scale preparation and characterization of recombinant ovine placental lactogen. J. Endocrinol. 152, 317-327 (1997).
    • (1997) J. Endocrinol. , vol.152 , pp. 317-327
    • Sakal, E.1
  • 16
    • 0032441098 scopus 로고    scopus 로고
    • Cloning, preparation, and characterization of biologically active recombinant caprine placental lactogen
    • Sakal, E., et al. Cloning, preparation, and characterization of biologically active recombinant caprine placental lactogen. J. Endocrinol. 159, 509-518 (1998).
    • (1998) J. Endocrinol. , vol.159 , pp. 509-518
    • Sakal, E.1
  • 17
    • 0030831289 scopus 로고    scopus 로고
    • Direct evidence that lactogenic hormones induce homodimerization of membrane-anchored prolactin receptor in intact Nb2-11C rat lymphoma cells
    • Sakal, E., Elberg, G. & Gertler, A. Direct evidence that lactogenic hormones induce homodimerization of membrane-anchored prolactin receptor in intact Nb2-11C rat lymphoma cells. FEBS Lett. 410, 289-292 (1997).
    • (1997) FEBS Lett. , vol.410 , pp. 289-292
    • Sakal, E.1    Elberg, G.2    Gertler, A.3
  • 18
    • 0024416653 scopus 로고
    • Cloning and expression of ovine placental lactogen
    • Colosi, P., et al. Cloning and expression of ovine placental lactogen. Mol. Endocrinol. 3, 1462-1469 (1989).
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1462-1469
    • Colosi, P.1
  • 19
    • 0032188942 scopus 로고    scopus 로고
    • Efficiency of signalling through cytokine receptors depends critically on receptor orientation
    • Syed, R.S. et al. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature 395, 511-516 (1998).
    • (1998) Nature , vol.395 , pp. 511-516
    • Syed, R.S.1
  • 20
    • 0029798402 scopus 로고    scopus 로고
    • Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å
    • Livnah, O. et al. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å. Science 273, 464-471 (1996).
    • (1996) Science , vol.273 , pp. 464-471
    • Livnah, O.1
  • 21
    • 0031739144 scopus 로고    scopus 로고
    • Structural basis for cytokine hormone-receptor recognition and receptor activation
    • Kossiakoff, A.A. & De Vos, A.M. Structural basis for cytokine hormone-receptor recognition and receptor activation. Adv. Protein Chem. 52, 67-108 (1998).
    • (1998) Adv. Protein Chem. , vol.52 , pp. 67-108
    • Kossiakoff, A.A.1    De Vos, A.M.2
  • 22
    • 0023411990 scopus 로고
    • Three-dimensional structure of a genetically engineered variant of porcine growth hormone
    • Abdel-Meguid, S.S. et al. Three-dimensional structure of a genetically engineered variant of porcine growth hormone. Proc. Natl. acad. Sci. USA 84, 6434-6437 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6434-6437
    • Abdel-Meguid, S.S.1
  • 23
    • 0028829622 scopus 로고
    • Biological activity and immunological reactivity of human prolactin mutants
    • Rhee, H.K. et al. Biological activity and immunological reactivity of human prolactin mutants. Endocrinology 136, 4990-49995 (1995).
    • (1995) Endocrinology , vol.136 , pp. 4990-49995
    • Rhee, H.K.1
  • 24
    • 0026748268 scopus 로고
    • Preparation, purification, and determination of the biological activities of 12 N terminus-truncated recombinant analogues of bovine placental lactogen
    • Gertler, A., et al. Preparation, purification, and determination of the biological activities of 12 N terminus-truncated recombinant analogues of bovine placental lactogen. J. Biol. Chem. 267, 12655-12659 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 12655-12659
    • Gertler, A.1
  • 25
    • 0026705352 scopus 로고
    • Identification of ligand binding determinants of the prolactin receptor
    • Rosakis-Adcock, M. & Kelley, P.A. Identification of ligand binding determinants of the prolactin receptor. J. Biol. Chem. 267, 7428-7433 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 7428-7433
    • Rosakis-Adcock, M.1    Kelley, P.A.2
  • 26
    • 0028032203 scopus 로고
    • The X-ray structure of the growth hormone-prolartin receptor complex
    • Somers, W., Ultsch, M., De Vos, A.M. & Kossiakoff, A.A. The X-ray structure of the growth hormone-prolartin receptor complex. Nature 372, 478-481 (1994).
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 27
    • 0027943660 scopus 로고
    • Comparison of the intermediate complexes of human growth hormone bound to the human growth hormone and prolactin receptors
    • Kossiakoff, A.A. et al. Comparison of the intermediate complexes of human growth hormone bound to the human growth hormone and prolactin receptors. Protein Sci. 3, 1697-1705 (1994).
    • (1994) Protein Sci. , vol.3 , pp. 1697-1705
    • Kossiakoff, A.A.1
  • 28
    • 0032783793 scopus 로고    scopus 로고
    • The structure, organization, activation and plasticity of the erythropoietin receptor
    • Wilson, I.A. & Jolliffe, L.K. The structure, organization, activation and plasticity of the erythropoietin receptor. Curr. Opin. Struct. Biol. 9, 696-704 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 696-704
    • Wilson, I.A.1    Jolliffe, L.K.2
  • 29
    • 0026335990 scopus 로고
    • Rational design of receptor-specific variants of human growth hormone
    • Cunningham, B.C. & Wells, J.A. Rational design of receptor-specific variants of human growth hormone. Proc. Natl. Acad. Sci. USA 88, 3407-3411 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3407-3411
    • Cunningham, B.C.1    Wells, J.A.2
  • 30
    • 0025615418 scopus 로고
    • Zinc mediation of the binding of human growth hormone to the human prolactin receptor
    • Cunningham, B.C., Bass, S., Fuh, G. & Wells, J.A. Zinc mediation of the binding of human growth hormone to the human prolactin receptor. Science 250, 1709-1712 (1990).
    • (1990) Science , vol.250 , pp. 1709-1712
    • Cunningham, B.C.1    Bass, S.2    Fuh, G.3    Wells, J.A.4
  • 31
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. & Wells, J.A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 32
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by ligand-induced conformation change science
    • Remy, I., Wilson, I.A. & Michnick, S.W. Erythropoietin receptor activation by ligand-induced conformation change science. Science 283, 990-993 (1999).
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 33
    • 0031766635 scopus 로고    scopus 로고
    • An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation
    • Livnah, O., et al. An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation. Nature Struct. Biol. 5, 993-1004 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 993-1004
    • Livnah, O.1
  • 34
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah, O. et al. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283, 987-990 (1999).
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1
  • 35
    • 0033583065 scopus 로고    scopus 로고
    • Ruminant placental lactogens act as antagonists to homologous growth hormone receptors and as agonists to human or rabbit growth hormone receptors
    • Herman, A., Helman, D., Livnah, O. & Gertler, A. Ruminant placental lactogens act as antagonists to homologous growth hormone receptors and as agonists to human or rabbit growth hormone receptors. J. Biol. Chem. 274, 7631-7639 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7631-7639
    • Herman, A.1    Helman, D.2    Livnah, O.3    Gertler, A.4
  • 36
    • 0028174290 scopus 로고
    • Prolactin-induced proliferation of Nb2 cells involves typrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2
    • Lebrun, J.J., Ali, S., Sofer, L., Ullrich, A. & Kelly, P.A. Prolactin-induced proliferation of Nb2 cells involves typrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2. J. Biol. Chem. 269, 14021-140266 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 14021-140266
    • Lebrun, J.J.1    Ali, S.2    Sofer, L.3    Ullrich, A.4    Kelly, P.A.5
  • 37
    • 0027179365 scopus 로고
    • Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase
    • Argetsinger, L. et al. Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 74, 237-244 (1993).
    • (1993) Cell , vol.74 , pp. 237-244
    • Argetsinger, L.1
  • 38
    • 0344573809 scopus 로고    scopus 로고
    • Growth hormone binding affinity for its receptor surpasses the requirements for cellular activity
    • Pearce, K.H., Cunningham, B.C., Fuh, G., Teeri, T. & Wells, J.A. Growth hormone binding affinity for its receptor surpasses the requirements for cellular activity. Biochemistry 38, 81-89 (1999).
    • (1999) Biochemistry , vol.38 , pp. 81-89
    • Pearce, K.H.1    Cunningham, B.C.2    Fuh, G.3    Teeri, T.4    Wells, J.A.5
  • 39
    • 0032212114 scopus 로고    scopus 로고
    • Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor
    • Christinger, H.W. et al. Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor. Acta Crystallogr. D 54, 1408-1411 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1408-1411
    • Christinger, H.W.1
  • 40
    • 0028103275 scopus 로고
    • CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 42
    • 0032488808 scopus 로고    scopus 로고
    • The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF.G9 complex
    • Huang, M. et al. The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF.G9 complex. J. Mol. Biol. 275, 873-894 (1998).
    • (1998) J. Mol. Biol. , vol.275 , pp. 873-894
    • Huang, M.1
  • 43
    • 0000275989 scopus 로고
    • Enhancement of the method of molecular replacement by incorporation of known structural information
    • Zhang, X.J. & Matthews, B.W. Enhancement of the method of molecular replacement by incorporation of known structural information. Acta Crystallogr. D 50, 675-686 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 675-686
    • Zhang, X.J.1    Matthews, B.W.2
  • 44
    • 0025862426 scopus 로고
    • The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast
    • Inaka, K., Taniyama, Y., Kikuchi, M., Morikawa, K. & Matsushima, M. The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast. J. Biol. Chem. 266, 12599-12603 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 12599-12603
    • Inaka, K.1    Taniyama, Y.2    Kikuchi, M.3    Morikawa, K.4    Matsushima, M.5
  • 45
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 46
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149 (1986).
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.1
  • 47
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400 (1971).
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 48
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwajj, R. & Honig, B. GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, A166 (1993).
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwajj, R.2    Honig, B.3


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