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Jacobson, L.O.1
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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.
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Spivak, J.L.1
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7
-
-
9444225791
-
-
note
-
X is any amino acid residue.
-
-
-
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8
-
-
0028838012
-
-
C.-H. Heldin, Cell 80, 213 (1995).
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Heldin, C.-H.1
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9
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0026332810
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B. C. Cunningham et al., Science 254, 821 (1991); G. Fuh et al., ibid. 256, 1677 (1992).
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Cunningham, B.C.1
-
10
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0026764441
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B. C. Cunningham et al., Science 254, 821 (1991); G. Fuh et al., ibid. 256, 1677 (1992).
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Science
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-
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Fuh, G.1
-
12
-
-
0030041323
-
-
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)].
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(1996)
Biochemistry
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, pp. 1681
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-
Philo, J.S.1
-
13
-
-
0027673149
-
-
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).
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Ihle, J.N.1
Quelle, F.W.2
Miura, O.3
-
14
-
-
0028956353
-
-
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).
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-
Klingmüller, U.1
Lorenz, U.2
Cantley, L.C.3
Neel, B.G.4
Lodish, H.F.5
-
15
-
-
9444236174
-
-
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)].
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(1996)
Science
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-
-
Wrighton, N.C.1
-
16
-
-
0027426950
-
-
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)].
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(1993)
Annu. Rev. Microbiol.
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, pp. 535
-
-
Hansen, J.N.1
-
17
-
-
9444294297
-
-
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
-
-
in preparation
-
E, A. Stura et al., in preparation.
-
-
-
Stura, E.A.1
-
21
-
-
9444285273
-
-
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
-
23
-
-
0028032203
-
-
W. Somers, M. Ultsch, A. M. De Vos, A. A. Kossiakoff, Nature 372, 478 (1994).
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Nature
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Somers, W.1
Ultsch, M.2
De Vos, A.M.3
Kossiakoff, A.A.4
-
24
-
-
0029067876
-
-
M. R. Walter et al., ibid. 376, 230 (1995).
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Nature
, vol.376
, pp. 230
-
-
Walter, M.R.1
-
25
-
-
0025198478
-
-
J.H. Wang et al., ibid 348, 411 (1990); S. E. Ryu et al., ibid., p. 419.
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(1990)
Nature
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-
-
Wang, J.H.1
-
26
-
-
9444265002
-
-
J.H. Wang et al., ibid 348, 411 (1990); S. E. Ryu et al., ibid., p. 419.
-
Nature
, pp. 419
-
-
Ryu, S.E.1
-
27
-
-
0028094639
-
-
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).
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-
-
Muller, Y.A.1
Ultsch, M.H.2
Kelley, R.F.3
De Vos, A.M.4
-
28
-
-
0028114236
-
-
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).
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Nature
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Harlos, K.1
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29
-
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0026490256
-
-
D. J. Leahy, W. A. Hendrickson, I. Aukhil, H. P. Erickson, Science 258, 987 (1992).
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Leahy, D.J.1
Hendrickson, W.A.2
Aukhil, I.3
Erickson, H.P.4
-
31
-
-
9444260100
-
-
note
-
118 are -50°, -27°; -76°, -21°; -99°, 26°; and -151°, 38°, respectively.
-
-
-
-
32
-
-
0000538815
-
-
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
-
-
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
-
-
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
-
-
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
-
-
note
-
The DPDPB crosslinker itself does not inactivate the EPO binding potential of EBP nor the proliferative properties of EMP1.
-
-
-
-
39
-
-
9444267397
-
-
D. L. Johnson et al., data not shown
-
D. L. Johnson et al., data not shown.
-
-
-
-
40
-
-
9444286714
-
-
_, in preparation
-
_, in preparation.
-
-
-
-
41
-
-
0027474991
-
-
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)].
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J. Mol. Biol.
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-
-
Adzhubei, A.A.1
Sternberg, M.J.2
-
42
-
-
0028351169
-
-
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)].
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(1994)
Neuron
, vol.12
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-
Huber, A.H.1
Wang, Y.E.2
Bieber, A.J.3
Bjorkman, P.J.4
-
43
-
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0027436998
-
-
R. A. Kumpf and D, A. Dougherty, Science 261, 1708 (1993); D. A. Dougherty, Science 271, 163 (1996).
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Kumpf, R.A.1
Dougherty, D.A.2
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44
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0030043489
-
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R. A. Kumpf and D, A. Dougherty, Science 261, 1708 (1993); D. A. Dougherty, Science 271, 163 (1996).
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Dougherty, D.A.1
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45
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0024260626
-
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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.
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Adv. Prot. Chem.
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-
-
Burley, S.K.1
Petsko, G.A.2
-
46
-
-
0028153795
-
-
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.
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J. Mol. Biol.
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-
-
Flocco, M.M.1
Mowbray, S.L.2
-
47
-
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0027237615
-
-
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
-
-
note
-
226 at position 5 still maintains an equivalent interaction.
-
-
-
-
49
-
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0028847977
-
-
A. Gustchina, A. Zdanov, C. Schalk-Hihi, A. Wlodawer, Proteins 21, 140 (1995).
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Gustchina, A.1
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Wlodawer, A.4
-
50
-
-
9444291014
-
-
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
-
-
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)].
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Baumgartner, J.W.1
Wells, C.A.2
Chen, C.M.3
Waters, M.J.4
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54
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-
0028147363
-
-
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)].
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Ronco, L.V.1
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55
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0025942918
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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)].
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Miyazaki, T.1
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0028963213
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D. J. Hilton, S. S. Watowich, P. J, Murray, H. F. Lodish, Proc. Natl. Acad. Sci. U.S.A. 92, 190 (1995); D. J. Hilton, S. S. Watowich, L. Katz, H. F. Lodish, J. Biol. Chem. 271, 4699 (1996).
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D. J. Hilton, S. S. Watowich, P. J, Murray, H. F. Lodish, Proc. Natl. Acad. Sci. U.S.A. 92, 190 (1995); D. J. Hilton, S. S. Watowich, L. Katz, H. F. Lodish, J. Biol. Chem. 271, 4699 (1996).
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58
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9444291013
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-
note
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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
-
-
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.
-
-
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60
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0026294507
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Wiley, Chichester
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Middleton, S.A.1
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9444270105
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note
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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.
-
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68
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0027297047
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J.-P. Boissel, W.-R. Lee, S. R. Presnell, F. E. Cohen, H. F. Bunn, J. Biol. Chem. 268, 15983 (1993).
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Jones, A.T.1
Zou, J.Y.2
Cowan, S.W.3
Kjeldgaard, M.4
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77
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9444238884
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note
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P4 substituted by a p-iodo-Phe are not shown.
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78
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84901961522
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A. T. Brünger, A. Krukowski, J. W. Erickson, Acta Crystallogr. A46, 585 (1990); A, T. Brünger, X-PLOR, Version 3.1: A System for X-rayand NMR (Yale Univ. Press, New Haven, 1992).
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(1990)
Acta Crystallogr.
, vol.A46
, pp. 585
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Brünger, A.T.1
Krukowski, A.2
Erickson, J.W.3
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79
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84901961522
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Yale Univ. Press, New Haven
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A. T. Brünger, A. Krukowski, J. W. Erickson, Acta Crystallogr. A46, 585 (1990); A, T. Brünger, X-PLOR, Version 3.1: A System for X-rayand NMR (Yale Univ. Press, New Haven, 1992).
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(1992)
X-PLOR, Version 3.1: A System for X-rayand NMR
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Brünger, A.T.1
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83
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9444235378
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note
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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.
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