메뉴 건너뛰기




Volumn 273, Issue 5274, 1996, Pages 464-471

Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPEPTIDE; ERYTHROPOIETIN RECEPTOR; HUMAN GROWTH HORMONE; PEPTIDE HORMONE;

EID: 0029798402     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5274.464     Document Type: Article
Times cited : (570)

References (83)
  • 1
    • 0026019106 scopus 로고
    • S. B. Krantz, Blood 77, 419 (1991); K. Jacobs et al., Nature 313, 806 (1985); L. O. Jacobson, E. Goldwasser, W. Fried, L. Pizak, ibid. 179, 633 (1957).
    • (1991) Blood , vol.77 , pp. 419
    • Krantz, S.B.1
  • 2
    • 0021978919 scopus 로고
    • S. B. Krantz, Blood 77, 419 (1991); K. Jacobs et al., Nature 313, 806 (1985); L. O. Jacobson, E. Goldwasser, W. Fried, L. Pizak, ibid. 179, 633 (1957).
    • (1985) Nature , vol.313 , pp. 806
    • Jacobs, K.1
  • 4
    • 0026317510 scopus 로고
    • P. Foa, Acta Haematol. 86, 162 (1991); J. L Spivak, Ed., Erythropoietin: Basic and Clinical Aspects (W. B. Saunders, Philadelphia, 1994), vol. 8, p. 863.
    • (1991) Acta Haematol. , vol.86 , pp. 162
    • Foa, P.1
  • 7
    • 9444225791 scopus 로고    scopus 로고
    • note
    • X is any amino acid residue.
  • 8
  • 9
    • 0026332810 scopus 로고
    • B. C. Cunningham et al., Science 254, 821 (1991); G. Fuh et al., ibid. 256, 1677 (1992).
    • (1991) Science , vol.254 , pp. 821
    • Cunningham, B.C.1
  • 10
    • 0026764441 scopus 로고
    • B. C. Cunningham et al., Science 254, 821 (1991); G. Fuh et al., ibid. 256, 1677 (1992).
    • (1992) Science , vol.256 , pp. 1677
    • Fuh, G.1
  • 12
    • 0030041323 scopus 로고    scopus 로고
    • o's for the first and second receptor molecules are of the order of nanomolar and micromolar, respectively [J. S. Philo et al., Biochemistry 35, 1681 (1996)].
    • (1996) Biochemistry , vol.35 , pp. 1681
    • Philo, J.S.1
  • 13
    • 0027673149 scopus 로고
    • J. N. Ihle, F. W. Quelle, O. Miura, Seminars Immunol. 5, 375 (1993); U. Klingmüller, U. Lorenz, L. C. Cantley, B. G. Neel, H. F. Lodish, Cell 80, 729 (1995).
    • (1993) Seminars Immunol. , vol.5 , pp. 375
    • Ihle, J.N.1    Quelle, F.W.2    Miura, O.3
  • 15
    • 9444236174 scopus 로고    scopus 로고
    • P17. A sequence search in the SWISS-PROT database shows that the primary structure of EMP1 shares a high sequence identity to a family of bacterial peptides that go through post-translational modifications to become lantibiotics [J. N. Hansen, Annu. Rev. Microbiol. 47, 535 (1993)].
    • (1996) Science , vol.273 , pp. 458
    • Wrighton, N.C.1
  • 16
    • 0027426950 scopus 로고
    • P17. A sequence search in the SWISS-PROT database shows that the primary structure of EMP1 shares a high sequence identity to a family of bacterial peptides that go through post-translational modifications to become lantibiotics [J. N. Hansen, Annu. Rev. Microbiol. 47, 535 (1993)].
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 535
    • Hansen, J.N.1
  • 17
    • 9444294297 scopus 로고    scopus 로고
    • note
    • Abbreviations for the amino acid residues are: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln: R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
  • 19
    • 9444221093 scopus 로고    scopus 로고
    • in preparation
    • E, A. Stura et al., in preparation.
    • Stura, E.A.1
  • 21
    • 9444285273 scopus 로고    scopus 로고
    • unpublished data
    • 2-terminal α helix exists in solution or is a crystallization packing artifact. This helical region is not observed in the known structures of hGHbp (begins at residue 32) (7), PRLR (begins at residue 2, without any defined secondary structure until the first β strand, residue 6) (17). the INF-γRα (begins at residue 17) (18), or tissue factor (begins at residue 3 without any defined secondary structure until the first β strand at residue 11) (20).
    • Livnah, O.1
  • 24
    • 0029067876 scopus 로고
    • M. R. Walter et al., ibid. 376, 230 (1995).
    • (1995) Nature , vol.376 , pp. 230
    • Walter, M.R.1
  • 25
    • 0025198478 scopus 로고
    • J.H. Wang et al., ibid 348, 411 (1990); S. E. Ryu et al., ibid., p. 419.
    • (1990) Nature , vol.348 , pp. 411
    • Wang, J.H.1
  • 26
    • 9444265002 scopus 로고    scopus 로고
    • J.H. Wang et al., ibid 348, 411 (1990); S. E. Ryu et al., ibid., p. 419.
    • Nature , pp. 419
    • Ryu, S.E.1
  • 28
    • 0028114236 scopus 로고
    • Y. A. Muller, M. H. Ultsch, R. F. Kelley, A. M. de Vos, Biochemistry 33, 10864 (1994); K. Harlos et al., Nature 370, 662 (1994).
    • (1994) Nature , vol.370 , pp. 662
    • Harlos, K.1
  • 31
    • 9444260100 scopus 로고    scopus 로고
    • note
    • 118 are -50°, -27°; -76°, -21°; -99°, 26°; and -151°, 38°, respectively.
  • 32
    • 0000538815 scopus 로고
    • The molecular surface areas buried by interaction were calculated with the use of the program MS [M. L. Connolly, J. Appl. Crystallogr. 16, 439 (1983)] with a 1.74 Å probe sphere and standard atomic radii [D. R. Davies, E. A. Padlan, S. Sheriff, Annu. Rev. Biochem. 59, 439 (1990)]. There may be some discrepancies between our values reported here and other (7) published values because we used a different algorithm [Connolly (above) compared to B. Lee and F. M. Richards, J. Mol. Biol. 55, 379 (1971)] and different probe radii. For clarity, all values reported here have been calculated in the same way for better comparison between the receptors.
    • (1983) J. Appl. Crystallogr. , vol.16 , pp. 439
    • Connolly, M.L.1
  • 33
    • 0025352392 scopus 로고
    • The molecular surface areas buried by interaction were calculated with the use of the program MS [M. L. Connolly, J. Appl. Crystallogr. 16, 439 (1983)] with a 1.74 Å probe sphere and standard atomic radii [D. R. Davies, E. A. Padlan, S. Sheriff, Annu. Rev. Biochem. 59, 439 (1990)]. There may be some discrepancies between our values reported here and other (7) published values because we used a different algorithm [Connolly (above) compared to B. Lee and F. M. Richards, J. Mol. Biol. 55, 379 (1971)] and different probe radii. For clarity, all values reported here have been calculated in the same way for better comparison between the receptors.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 439
    • Davies, D.R.1    Padlan, E.A.2    Sheriff, S.3
  • 34
    • 0015222647 scopus 로고
    • The molecular surface areas buried by interaction were calculated with the use of the program MS [M. L. Connolly, J. Appl. Crystallogr. 16, 439 (1983)] with a 1.74 Å probe sphere and standard atomic radii [D. R. Davies, E. A. Padlan, S. Sheriff, Annu. Rev. Biochem. 59, 439 (1990)]. There may be some discrepancies between our values reported here and other (7) published values because we used a different algorithm [Connolly (above) compared to B. Lee and F. M. Richards, J. Mol. Biol. 55, 379 (1971)] and different probe radii. For clarity, all values reported here have been calculated in the same way for better comparison between the receptors.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379
    • Lee, B.1    Richards, F.M.2
  • 37
    • 9444252591 scopus 로고    scopus 로고
    • note
    • P11 has a hydrogen bond to EBP distorting the ψ value from its normal 0° ± 30° (i + 2) in a standard type I β turn.
  • 38
    • 9444297563 scopus 로고    scopus 로고
    • note
    • The DPDPB crosslinker itself does not inactivate the EPO binding potential of EBP nor the proliferative properties of EMP1.
  • 39
    • 9444267397 scopus 로고    scopus 로고
    • D. L. Johnson et al., data not shown
    • D. L. Johnson et al., data not shown.
  • 40
    • 9444286714 scopus 로고    scopus 로고
    • _, in preparation
    • _, in preparation.
  • 41
    • 0027474991 scopus 로고
    • 213 have φ, ψ = -68°, 142°; -75°, -174°; -80°, 162°; -80°, 162°; -70°, 167°, and -95°, 169°, respectively. The presence of a polyproline helical conformation in an FBN III domain was first noted in the structure of Drosophila neuroglian [A. H, Huber, Y. E. Wang, A J. Bieber, P. J. Bjorkman, Neuron 12, 717 (1994)].
    • (1993) J. Mol. Biol. , vol.229 , pp. 472
    • Adzhubei, A.A.1    Sternberg, M.J.2
  • 42
    • 0028351169 scopus 로고
    • 213 have φ, ψ = -68°, 142°; -75°, -174°; -80°, 162°; -80°, 162°; -70°, 167°, and -95°, 169°, respectively. The presence of a polyproline helical conformation in an FBN III domain was first noted in the structure of Drosophila neuroglian [A. H, Huber, Y. E. Wang, A J. Bieber, P. J. Bjorkman, Neuron 12, 717 (1994)].
    • (1994) Neuron , vol.12 , pp. 717
    • Huber, A.H.1    Wang, Y.E.2    Bieber, A.J.3    Bjorkman, P.J.4
  • 43
    • 0027436998 scopus 로고
    • R. A. Kumpf and D, A. Dougherty, Science 261, 1708 (1993); D. A. Dougherty, Science 271, 163 (1996).
    • (1993) Science , vol.261 , pp. 1708
    • Kumpf, R.A.1    Dougherty, D.A.2
  • 44
    • 0030043489 scopus 로고    scopus 로고
    • R. A. Kumpf and D, A. Dougherty, Science 261, 1708 (1993); D. A. Dougherty, Science 271, 163 (1996).
    • (1996) Science , vol.271 , pp. 163
    • Dougherty, D.A.1
  • 45
    • 0024260626 scopus 로고
    • 207 in leucine aminopeptidase [H. Kim and W. N. Lipscomb, Biochemistry 32, 8465 (1993)], but these systems are not well aligned as in the cytokine receptor structures.
    • (1988) Adv. Prot. Chem. , vol.39 , pp. 125
    • Burley, S.K.1    Petsko, G.A.2
  • 46
    • 0028153795 scopus 로고
    • 207 in leucine aminopeptidase [H. Kim and W. N. Lipscomb, Biochemistry 32, 8465 (1993)], but these systems are not well aligned as in the cytokine receptor structures.
    • (1994) J. Mol. Biol. , vol.235 , pp. 709
    • Flocco, M.M.1    Mowbray, S.L.2
  • 47
    • 0027237615 scopus 로고
    • 207 in leucine aminopeptidase [H. Kim and W. N. Lipscomb, Biochemistry 32, 8465 (1993)], but these systems are not well aligned as in the cytokine receptor structures.
    • (1993) Biochemistry , vol.32 , pp. 8465
    • Kim, H.1    Lipscomb, W.N.2
  • 48
    • 9444258902 scopus 로고    scopus 로고
    • note
    • 226 at position 5 still maintains an equivalent interaction.
  • 50
    • 9444291014 scopus 로고    scopus 로고
    • note
    • Although IFN-γRa and tissue factor do not have a WSXWS motif, the corresponding sequences TTEKS (residues 213 to 217) for IFN-γRα (18) and KSTDS (residues 201 to 205) for tissue factor (20), maintain a very similar β bulge.
  • 53
    • 0028052289 scopus 로고
    • 226 to Ala mutation also abrogates hGHR binding to hGH, and its expression on the cell surface is drastically reduced [J. W. Baumgartner, C. A. Wells, C. M. Chen, M. J. Waters, J. Biol. Chem. 269, 29094 (1994)]. In GM-CSFRα and IL-2Rβ, point mutations of the serine residues cause a substantial decrease in cell surface expression but have little or no effect on ligand binding [L. V. Ronco et al., J. Biol. Chem. 269, 277 (1994); T. Miyazaki, M. Maruyama, G. Yamada, M. Hatakeyama, T. Taniguchi, EMBO J. 10, 3191 (1991)].
    • (1994) J. Biol. Chem. , vol.269 , pp. 29094
    • Baumgartner, J.W.1    Wells, C.A.2    Chen, C.M.3    Waters, M.J.4
  • 54
    • 0028147363 scopus 로고
    • 226 to Ala mutation also abrogates hGHR binding to hGH, and its expression on the cell surface is drastically reduced [J. W. Baumgartner, C. A. Wells, C. M. Chen, M. J. Waters, J. Biol. Chem. 269, 29094 (1994)]. In GM-CSFRα and IL-2Rβ, point mutations of the serine residues cause a substantial decrease in cell surface expression but have little or no effect on ligand binding [L. V. Ronco et al., J. Biol. Chem. 269, 277 (1994); T. Miyazaki, M. Maruyama, G. Yamada, M. Hatakeyama, T. Taniguchi, EMBO J. 10, 3191 (1991)].
    • (1994) J. Biol. Chem. , vol.269 , pp. 277
    • Ronco, L.V.1
  • 55
    • 0025942918 scopus 로고
    • 226 to Ala mutation also abrogates hGHR binding to hGH, and its expression on the cell surface is drastically reduced [J. W. Baumgartner, C. A. Wells, C. M. Chen, M. J. Waters, J. Biol. Chem. 269, 29094 (1994)]. In GM-CSFRα and IL-2Rβ, point mutations of the serine residues cause a substantial decrease in cell surface expression but have little or no effect on ligand binding [L. V. Ronco et al., J. Biol. Chem. 269, 277 (1994); T. Miyazaki, M. Maruyama, G. Yamada, M. Hatakeyama, T. Taniguchi, EMBO J. 10, 3191 (1991)].
    • (1991) EMBO J. , vol.10 , pp. 3191
    • Miyazaki, T.1    Maruyama, M.2    Yamada, G.3    Hatakeyama, M.4    Taniguchi, T.5
  • 58
    • 9444291013 scopus 로고    scopus 로고
    • note
    • Modeling and docking experiments of possible interactions between the two D2 domains of EBP did not provide a definitive answer as to how EBP1 and EBP2 might interact in the EPO-EBP complex.
  • 59
    • 9444296813 scopus 로고    scopus 로고
    • note
    • In EBP, the L5 loop is three residues shorter than in hGHbp and PRLR, whereas the EBP L6 loop is three and four residues longer than in hGHbp and PRLR, respectively. The L2 loop also varies (six to ten residues) among the three receptors, but in EBP does not participate in peptide binding; in hGHbp, the L2 loop is partially disordered although it does contact the hormone.
  • 60
    • 0026294507 scopus 로고
    • Wiley, Chichester
    • I. A. Wilson et al., in Ciba Foundation Symp. (Wiley, Chichester, 1991), vol. 159, p. 13.
    • (1991) Ciba Foundation Symp. , vol.159 , pp. 13
    • Wilson, I.A.1
  • 61
    • 0028260226 scopus 로고
    • J. A. Wells, Curr, Opin. Cell Biol. 6, 163 (1994); T. Clackson and J. A. Wells, Science 267, 383 (1995); J. A. Wells, Proc. Natl. Acad. Sci. U.S.A. 93, 1 (1996).
    • (1994) Curr, Opin. Cell Biol. , vol.6 , pp. 163
    • Wells, J.A.1
  • 62
    • 0028916599 scopus 로고
    • J. A. Wells, Curr, Opin. Cell Biol. 6, 163 (1994); T. Clackson and J. A. Wells, Science 267, 383 (1995); J. A. Wells, Proc. Natl. Acad. Sci. U.S.A. 93, 1 (1996).
    • (1995) Science , vol.267 , pp. 383
    • Clackson, T.1    Wells, J.A.2
  • 63
    • 0030050701 scopus 로고    scopus 로고
    • J. A. Wells, Curr, Opin. Cell Biol. 6, 163 (1994); T. Clackson and J. A. Wells, Science 267, 383 (1995); J. A. Wells, Proc. Natl. Acad. Sci. U.S.A. 93, 1 (1996).
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1
    • Wells, J.A.1
  • 64
    • 0029055793 scopus 로고
    • L K. Jolliffe et al., Nephrol. Dial. Trans. 10, suppl. 2, 28 (1995); S. A. Middleton et al., J. Biol. Chem. 271, 14045 (1996).
    • (1995) Nephrol. Dial. Trans. , vol.10 , Issue.2 SUPPL. , pp. 28
    • Jolliffe, L.K.1
  • 65
    • 0029975623 scopus 로고    scopus 로고
    • L K. Jolliffe et al., Nephrol. Dial. Trans. 10, suppl. 2, 28 (1995); S. A. Middleton et al., J. Biol. Chem. 271, 14045 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 14045
    • Middleton, S.A.1
  • 66
    • 9444270105 scopus 로고    scopus 로고
    • note
    • These correspond to residues 164 to 166 in EBP1 and 133 to 135 in EBP2, residues 55 to 58, 73 to 78 in hGHbp1, and 54 to 60, 73 to 75 for hGHbp2, and residues 31 to 33, 84 to 86 in PRLR.
  • 69
    • 0026577197 scopus 로고
    • S. S. Watowich et al., Proc. Natl. Acad. Sci. U.S.A. 89, 2140 (1992); S. S. Watowich, D. J. Hilton, H. F. Lodish, Mol. Cell Biol. 14, 3535 (1994).
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2140
    • Watowich, S.S.1
  • 74
    • 0002452464 scopus 로고
    • L. Sawyer, N. Isaacs, S. Bailey, Eds. SERC Darsbury Laboratory, Warrington
    • Z. Otwinowski, in Data Collection and Processing, L. Sawyer, N. Isaacs, S. Bailey, Eds. (SERC Darsbury Laboratory, Warrington, 1993), pp. 56.
    • (1993) Data Collection and Processing , pp. 56
    • Otwinowski, Z.1
  • 77
    • 9444238884 scopus 로고    scopus 로고
    • note
    • P4 substituted by a p-iodo-Phe are not shown.
  • 83
    • 9444235378 scopus 로고    scopus 로고
    • note
    • We thank A. M. DeVos for hGH-PRLR coordinates, M. R. Walter for IFN-γRα-IFN-γ coordinates, M. Pique for help in preparing Fig. 6, E. Tsao and K. Frame for fermentations, F. McMahon for technical assistance, and K. Hoey for peptide synthesis. Supported in part by NIH grant GM-49497 (I.A.W.) and the Rueff-Wormser Scholarship Fund (O.L.). This is publication 9888-MB from the Scripps Research Institute. This article is dedicated to the memory of our colleague Jairo H. Arévalo.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.