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Volumn 33, Issue 4 SUPPL., 2002, Pages

Crystal structures of α-helical cytokine-receptor complexes: We've only scratched the surface

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLOGRAPHY; ENZYMES; MOLECULAR BIOLOGY;

EID: 0036793231     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (18)

References (80)
  • 2
    • 0033554674 scopus 로고    scopus 로고
    • Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme
    • Aritomi, M., N. Kunishima, T. Okamoto, R. Kuroki, Y. Ota, and K. Morikawa. 1999. Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme. Nature 401:713-717.
    • (1999) Nature , vol.401 , pp. 713-717
    • Aritomi, M.1    Kunishima, N.2    Okamoto, T.3    Kuroki, R.4    Ota, Y.5    Morikawa, K.6
  • 3
    • 0025356737 scopus 로고
    • Shared architecture of hormone binidng in type I and type II interferon receptors
    • Bazan, J.F. 1990. Shared architecture of hormone binidng in type I and type II interferon receptors. Cell 61:753-754.
    • (1990) Cell , vol.61 , pp. 753-754
    • Bazan, J.F.1
  • 4
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J.F. 1990. Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87:6934-413.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 5
    • 0026763387 scopus 로고
    • Unraveling the structure of IL-2
    • Bazan, J.F. 1992. Unraveling the structure of IL-2. Science 257:410-413.
    • (1992) Science , vol.257 , pp. 410-413
    • Bazan, J.F.1
  • 6
    • 0033571455 scopus 로고    scopus 로고
    • Producing selenomethionine-labeled proteins with a baculovirus expression vector system
    • Bellizzi, J.J., J. Widom, C.W. Kemp, and J. Clardy. 1999. Producing selenomethionine-labeled proteins with a baculovirus expression vector system. Structure Fold Des. 7:R263-267.
    • (1999) Structure Fold Des. , vol.7
    • Bellizzi, J.J.1    Widom, J.2    Kemp, C.W.3    Clardy, J.4
  • 7
    • 0032536814 scopus 로고    scopus 로고
    • Crystal structure of a cytokine-binding region of gp130
    • Bravo, J., D. Staunton, J.K. Heath, and E.Y. Jones. 1998. Crystal structure of a cytokine-binding region of gp130. EMBO J. 17:1665-1674.
    • (1998) EMBO J. , vol.17 , pp. 1665-1674
    • Bravo, J.1    Staunton, D.2    Heath, J.K.3    Jones, E.Y.4
  • 8
    • 0035896394 scopus 로고    scopus 로고
    • Structure of an extracellular gp130 cytokine receptor signaling complex
    • Chow, D., X. He, A.L. Snow, S. Rose-John, and K.C. Garcia. 2001. Structure of an extracellular gp130 cytokine receptor signaling complex. Science 291:2150-2155.
    • (2001) Science , vol.291 , pp. 2150-2155
    • Chow, D.1    He, X.2    Snow, A.L.3    Rose-John, S.4    Garcia, K.C.5
  • 9
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity
    • Clackson, T., M.H. Ultsch, J.A. Wells, and A.M. de Vos. 1998. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277:1111-1128.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    De Vos, A.M.4
  • 10
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. and J.A. Wells. 1995. A hot spot of binding energy in a hormone-receptor interface. Science 267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 11
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham, B.C., M. Ultsch, A.M. De Vos, M.G. Mulkerrin, K.R. Clauser, and J.A. Wells. 199 1. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254:821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 12
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • Cunningham, B.C. and J.A. Wells. 1993. Comparison of a structural and a functional epitope. J. Mol. Biol. 234:554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 15
    • 0034142070 scopus 로고    scopus 로고
    • Novel approach to phasing proteins: Derivatization by short cryo-soaking with halides
    • Dauter, Z., M. Dauter, and K.R. Rajashankar. 2000. Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr. D Biol. Crystallogr. 56(Pt 2):232-237.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , Issue.PART 2 , pp. 232-237
    • Dauter, Z.1    Dauter, M.2    Rajashankar, K.R.3
  • 16
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos, A.M., M. Ultsch, and A.A. Kossiakoff. 1992. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255:306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 18
    • 0026320870 scopus 로고
    • Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor
    • Diederichs, K., T. Boone, and P.A. Karplus. 1991. Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor. Science 254:1779-1782.
    • (1991) Science , vol.254 , pp. 1779-1782
    • Diederichs, K.1    Boone, T.2    Karplus, P.A.3
  • 21
    • 0026764441 scopus 로고
    • Rational design of potent antagonists to the human growth hormone receptor
    • Fuh, G., B.C. Cunningham, R. Fukunaga, S. Nagata, D.V. Goeddel, and J.A. Wells. 1992. Rational design of potent antagonists to the human growth hormone receptor. Science 256:1677-1680.
    • (1992) Science , vol.256 , pp. 1677-1680
    • Fuh, G.1    Cunningham, B.C.2    Fukunaga, R.3    Nagata, S.4    Goeddel, D.V.5    Wells, J.A.6
  • 23
    • 0033574713 scopus 로고    scopus 로고
    • Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface
    • Hage, T., W. Sebald, and P. Reinemer. 1999. Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface. Cell 97:271-281.
    • (1999) Cell , vol.97 , pp. 271-281
    • Hage, T.1    Sebald, W.2    Reinemer, P.3
  • 24
    • 0030783379 scopus 로고    scopus 로고
    • Phasing methods for protein crystallography
    • Hauptman, H. 1997. Phasing methods for protein crystallography. Curr. Opin. Struct. Biol. 7:672-680.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 672-680
    • Hauptman, H.1
  • 25
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C.H. 1995. Dimerization of cell surface receptors in signal transduction. Cell 80:213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 26
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. 1991. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254:51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 27
    • 0034387005 scopus 로고    scopus 로고
    • Synchrotron crystallography
    • Hendrickson, W.A. 2000. Synchrotron crystallography. Trends Biochem. Sci. 25:637-643.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 637-643
    • Hendrickson, W.A.1
  • 28
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W.A., J.R. Horton, and D.M. LeMaster. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 29
    • 0024219852 scopus 로고
    • Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation
    • Hendrickson, W.A., J.L. Smith, R.P. Phizackerley, and E.A. Merritt. 1988. Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation. Proteins 4:77-88.
    • (1988) Proteins , vol.4 , pp. 77-88
    • Hendrickson, W.A.1    Smith, J.L.2    Phizackerley, R.P.3    Merritt, E.A.4
  • 30
    • 0034456782 scopus 로고    scopus 로고
    • Growth hormone receptor antagonist therapy in acromegalic patients resistant to somatostatin analogs
    • Herman-Bonert, V.S., K. Zib, J.A. Scarlett, and S. Melmed. 2000. Growth hormone receptor antagonist therapy in acromegalic patients resistant to somatostatin analogs. J. Clin. Endocrinol. Metab. 85:295-2961.
    • (2000) J. Clin. Endocrinol. Metab. , vol.85 , pp. 295-2961
    • Herman-Bonert, V.S.1    Zib, K.2    Scarlett, J.A.3    Melmed, S.4
  • 31
    • 84944510121 scopus 로고
    • Cryocrystallography of biological macromolecules: A generally applicable method
    • Hope, H. 1988. Cryocrystallography of biological macromolecules: a generally applicable method. Acta Crystallogr. B 44(Pt 1):22-26.
    • (1988) Acta Crystallogr. B , vol.44 , Issue.PART 1 , pp. 22-26
    • Hope, H.1
  • 32
    • 0026206788 scopus 로고
    • Sparse Matrix Sampling: A screening method for crystallization of proteins
    • Jancarik, J.J. and S.H. Kim. 1991. Sparse Matrix Sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24-409.
    • (1991) J. Appl. Crystallogr. , pp. 24-409
    • Jancarik, J.J.1    Kim, S.H.2
  • 33
    • 0032539954 scopus 로고    scopus 로고
    • Identification of a 13 amino acid peptide mimetic of erythropoietin and description of amino acids critical for the mimetic activity of EMP1
    • Johnson, D.L., F.X. Farrell, F.P. Barbone, F.J. McMahon, J. Tullai, K. Hoey, O. Livnah, N.C. Wrighton, et al. 1998. Identification of a 13 amino acid peptide mimetic of erythropoietin and description of amino acids critical for the mimetic activity of EMP1. Biochemistry 37:3699-3710.
    • (1998) Biochemistry , vol.37 , pp. 3699-3710
    • Johnson, D.L.1    Farrell, F.X.2    Barbone, F.P.3    McMahon, F.J.4    Tullai, J.5    Hoey, K.6    Livnah, O.7    Wrighton, N.C.8
  • 36
    • 0036065431 scopus 로고    scopus 로고
    • Non-competitive antibody neutralization of IL-10 revealed by protein engineering and X-ray crystallography
    • Josephson, K., B.C. Jones, L.J. Walter, R. DiGiacomo, S.R. Indelicato, and M.R. Walter. 2002. Non-competitive antibody neutralization of IL-10 revealed by protein engineering and X-ray crystallography. Structure 10:981-987.
    • (2002) Structure , vol.10 , pp. 981-987
    • Josephson, K.1    Jones, B.C.2    Walter, L.J.3    DiGiacomo, R.4    Indelicato, S.R.5    Walter, M.R.6
  • 37
    • 0034897552 scopus 로고    scopus 로고
    • Crystal structure of the IL-10/IL-10R1 complex reveals shared receptor binding site
    • Josephson, K., N.J. Logsdon, and M.R. Walter. 2001. Crystal structure of the IL-10/IL-10R1 complex reveals shared receptor binding site. Immunity 15:35-46.
    • (2001) Immunity , vol.15 , pp. 35-46
    • Josephson, K.1    Logsdon, N.J.2    Walter, M.R.3
  • 38
    • 0035214095 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction of a complex between IL-10 and soluble IL-10R1
    • Josephson, K., D.T. McPherson, and M.R. Walter. 2001. Purification, crystallization and preliminary X-ray diffraction of a complex between IL-10 and soluble IL-10R1. Acta Crystallogr. D Biol. Crystallogr. 57:1908-1911.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1908-1911
    • Josephson, K.1    McPherson, D.T.2    Walter, M.R.3
  • 40
    • 0037138370 scopus 로고    scopus 로고
    • Signaling through the JAK/STAT pathway, recent advances and future challenges
    • Kisseleva, T., S. Bhattacharya, J. Braunstein, and C.W. Schindler. 2002. Signaling through the JAK/STAT pathway, recent advances and future challenges. Gene 285:1-24.
    • (2002) Gene , vol.285 , pp. 1-24
    • Kisseleva, T.1    Bhattacharya, S.2    Braunstein, J.3    Schindler, C.W.4
  • 41
    • 0033548254 scopus 로고    scopus 로고
    • Probability analysis of variational crystallization and its application to gp 120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1)
    • Kwong, P.D., R. Wyatt, E. Desjardins, J. Robinson, J.S. Culp, B.D. Hellmig, R.W. Sweet, J. Sodroski, et al. 1999. Probability analysis of variational crystallization and its application to gp 120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J. Biol. Chem. 274:4115-4123.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4115-4123
    • Kwong, P.D.1    Wyatt, R.2    Desjardins, E.3    Robinson, J.4    Culp, J.S.5    Hellmig, B.D.6    Sweet, R.W.7    Sodroski, J.8
  • 42
    • 0033762983 scopus 로고    scopus 로고
    • Current state of automated crystallographic data analysis
    • Lamzin, V.S. and A. Perrakis. 2000. Current state of automated crystallographic data analysis. Nat. Struct. Biol. 7 (Suppl):978-981.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 978-981
    • Lamzin, V.S.1    Perrakis, A.2
  • 44
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah, O., E.A. Stura, S.A. Middleton, D.L. Johnson, L.K. Jolliffe, and I.A. Wilson. 1999. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283:987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 45
    • 0027136111 scopus 로고
    • Affinity maturation of human growth hormone by monovalent phage display
    • Lowman, H.B. and J.A. Wells. 1993. Affinity maturation of human growth hormone by monovalent phage display. J. Mol. Biol. 234:564-578.
    • (1993) J. Mol. Biol. , vol.234 , pp. 564-578
    • Lowman, H.B.1    Wells, J.A.2
  • 46
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5
    • Milburn, M.V., A.M. Hassell, M.H. Lambert, S.R. Jordan, A.E. Proudfoot, P. Graber, and T.N. Wells. 1993. A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5. Nature 363:172-176.
    • (1993) Nature , vol.363 , pp. 172-176
    • Milburn, M.V.1    Hassell, A.M.2    Lambert, M.H.3    Jordan, S.R.4    Proudfoot, A.E.5    Graber, P.6    Wells, T.N.7
  • 48
    • 0034940904 scopus 로고    scopus 로고
    • Protein crystal structure solution by fast incorporation of negatively and positively charged anomalous scatterers
    • Nagem, R.A., Z. Dauter, and I. Polikarpov. 2001. Protein crystal structure solution by fast incorporation of negatively and positively charged anomalous scatterers. Acta Crystallogr. D Biol. Crystallogr. 57:996-1002.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 996-1002
    • Nagem, R.A.1    Dauter, Z.2    Polikarpov, I.3
  • 49
    • 0036233585 scopus 로고    scopus 로고
    • Cytokine signaling in 2002: New surprises in the Jak/Stat pathway
    • O'Shea, J.J., M. Gadina, and R.D. Schreiber. 2002. Cytokine signaling in 2002: new surprises in the Jak/Stat pathway. Cell 109 (Suppl):S121-131.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • O'Shea, J.J.1    Gadina, M.2    Schreiber, R.D.3
  • 50
    • 0026727235 scopus 로고
    • Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor
    • Pandit, J., A. Bohm, J. Jancarik, R. Halenbeck, K. Koths, and S.H. Kim. 1992. Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor. Science 258:1358-1362.
    • (1992) Science , vol.258 , pp. 1358-1362
    • Pandit, J.1    Bohm, A.2    Jancarik, J.3    Halenbeck, R.4    Koths, K.5    Kim, S.H.6
  • 53
    • 0035091323 scopus 로고    scopus 로고
    • The structure and activity of a monomeric interferon-gamma:alpha-chain receptor signaling complex
    • Randal, M. and A.A. Kossiakoff. 2001. The structure and activity of a monomeric interferon-gamma:alpha-chain receptor signaling complex. Structure (Camb.) 9:155-163.
    • (2001) Structure (Camb.) , vol.9 , pp. 155-163
    • Randal, M.1    Kossiakoff, A.A.2
  • 54
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., I.A. Wilson and S.W. Michnick. 1999. Erythropoietin receptor activation by a ligand-induced conformation change. Science 283:990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 57
    • 0028774714 scopus 로고
    • Corocrystallography
    • Rodgers, D.W. 1994. Corocrystallography. Structure 2:1135-1140.
    • (1994) Structure , vol.2 , pp. 1135-1140
    • Rodgers, D.W.1
  • 59
    • 0031041014 scopus 로고    scopus 로고
    • 1.9 A crystal structure of intetleukin 6: Implications for a novel mode of receptor dimerization and signaling
    • Somers, W., M. Stahl, and J.S. Seehra. 1997. 1.9 A crystal structure of intetleukin 6: implications for a novel mode of receptor dimerization and signaling. EMBO J 16:989-997.
    • (1997) EMBO J. , vol.16 , pp. 989-997
    • Somers, W.1    Stahl, M.2    Seehra, J.S.3
  • 60
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • Somers, W., M. Ultsch, A.M. De Vos, and A.A. Kossiakoff. 1994. The X-ray structure of a growth hormone-prolactin receptor complex. Nature 372:478-481.
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 61
    • 0027145507 scopus 로고
    • Cytokine structural taxonomy and mechanisms of receptor engagement
    • Sprang, S.R. and J.F. Bazan. 1993. Cytokine structural taxonomy and mechanisms of receptor engagement. Curr. Opin. Struct. Biol. 3:815-821.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 815-821
    • Sprang, S.R.1    Bazan, J.F.2
  • 62
    • 0033794367 scopus 로고    scopus 로고
    • High-throughput protein crystallization
    • Stevens, R.C. 2000. High-throughput protein crystallization. Curr. Opin. Struct. Biol. 10:558-563.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 558-563
    • Stevens, R.C.1
  • 63
    • 0032188942 scopus 로고    scopus 로고
    • Efficiency of signalling through cytokine receptors depends critically on receptor orientation
    • Syed, R.S., S.W. Reid, C. Li, J.C. Cheetham, K.H. Aoki, B. Liu, H. Zhan, T.D. Osslund, et al. 1998. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature 395:511-516.
    • (1998) Nature , vol.395 , pp. 511-516
    • Syed, R.S.1    Reid, S.W.2    Li, C.3    Cheetham, J.C.4    Aoki, K.H.5    Liu, B.6    Zhan, H.7    Osslund, T.D.8
  • 69
    • 0026520373 scopus 로고
    • Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor
    • Walter, M.R., W.J. Cook, S.E. Ealick, T.L. Nagabhushan, P.P. Trotta, and C.E. Bugg. 1992. Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor. J. Mol. Biol. 224:1075-1085.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1075-1085
    • Walter, M.R.1    Cook, W.J.2    Ealick, S.E.3    Nagabhushan, T.L.4    Trotta, P.P.5    Bugg, C.E.6
  • 71
    • 0029148581 scopus 로고
    • Crystal structure of interleukin 10 reveals an interferon gamma-like fold
    • Walter, M.R. and T.L. Nagabhushan. 1995. Crystal structure of interleukin 10 reveals an interferon gamma-like fold. Biochemistry 34:12118-12125.
    • (1995) Biochemistry , vol.34 , pp. 12118-12125
    • Walter, M.R.1    Nagabhushan, T.L.2
  • 76
    • 0033301681 scopus 로고    scopus 로고
    • New strategies for protein crystal growth
    • Wiencek, J.M. 1999. New strategies for protein crystal growth. Annu. Rev. Biomed. Eng. 1:505-534.
    • (1999) Annu. Rev. Biomed. Eng. , vol.1 , pp. 505-534
    • Wiencek, J.M.1
  • 78
    • 0034679726 scopus 로고    scopus 로고
    • Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12
    • Yoon, C., S.C. Johnston, J. Tang, M. Stahl, J.F. Tobin, and W.S. Somers. 2000. Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12. EMBO J. 19:3530-3541.
    • (2000) EMBO J. , vol.19 , pp. 3530-3541
    • Yoon, C.1    Johnston, S.C.2    Tang, J.3    Stahl, M.4    Tobin, J.F.5    Somers, W.S.6
  • 79
    • 0029644946 scopus 로고
    • Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma
    • Zdanov, A., C. Schalk-Hihi, A. Gustchina, M. Tsang, J. Weatherbee, and A. Wlodawer. 1995. Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma. Structure 3:591-601.
    • (1995) Structure , vol.3 , pp. 591-601
    • Zdanov, A.1    Schalk-Hihi, C.2    Gustchina, A.3    Tsang, M.4    Weatherbee, J.5    Wlodawer, A.6


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