메뉴 건너뛰기




Volumn 94, Issue 5, 2008, Pages 1754-1765

Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; CROSS LINKING REAGENT; CYTOKINE; GLUTARALDEHYDE; INTERLEUKIN 10; INTERLEUKIN 22; INTERLEUKIN 22 RECEPTOR; INTERLEUKIN DERIVATIVE; INTERLEUKIN RECEPTOR; INTERLEUKIN-22; INTERLEUKIN-22 RECEPTOR; UNCLASSIFIED DRUG;

EID: 41449114478     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.112664     Document Type: Article
Times cited : (43)

References (58)
  • 1
    • 33749983749 scopus 로고    scopus 로고
    • Interleukin-22: A novel T- and NK-cell derived cytokine that regulates the biology of tissue cells
    • Wolk, K., and R. Sabat. 2006. Interleukin-22: a novel T- and NK-cell derived cytokine that regulates the biology of tissue cells. Cytokine Growth Factor Rev. 17:367-380.
    • (2006) Cytokine Growth Factor Rev , vol.17 , pp. 367-380
    • Wolk, K.1    Sabat, R.2
  • 6
    • 0034565220 scopus 로고    scopus 로고
    • IL-TIF/IL-22: Genomic organization and mapping of the human and mouse genes
    • Dumoutier, L., E. Van Roost, G. Ameye, L. Michaux, and J. C. Renauld. 2000. IL-TIF/IL-22: genomic organization and mapping of the human and mouse genes. Genes Immun. 1:488-494.
    • (2000) Genes Immun , vol.1 , pp. 488-494
    • Dumoutier, L.1    Van Roost, E.2    Ameye, G.3    Michaux, L.4    Renauld, J.C.5
  • 7
    • 1642432084 scopus 로고    scopus 로고
    • The Class II cytokine receptor (CRF2) family: Overview and patterns of receptor-ligand interactions
    • Langer, J. A., E. C. Cutrone, and S. Kotenko. 2004. The Class II cytokine receptor (CRF2) family: overview and patterns of receptor-ligand interactions. Cytokine Growth Factor Rev. 15:33-48.
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 33-48
    • Langer, J.A.1    Cutrone, E.C.2    Kotenko, S.3
  • 10
    • 0035091323 scopus 로고    scopus 로고
    • The structure and activity of a monomeric interferon-γ:α-chain receptor signaling complex
    • Randal, M., and A. A. Kossiakoff. 2001. The structure and activity of a monomeric interferon-γ:α-chain receptor signaling complex. Structure. 9:155-163.
    • (2001) Structure , vol.9 , pp. 155-163
    • Randal, M.1    Kossiakoff, A.A.2
  • 11
    • 0034897552 scopus 로고    scopus 로고
    • Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site
    • Josephson, K., N. J. Logsdon, and M. R. Walter. 2001. Crystal structure of the IL-10/IL-10R1 complex reveals a 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
  • 13
    • 0035951795 scopus 로고    scopus 로고
    • Identification of the functional interleukin-22 (IL-22) receptor complex: The IL-10R2 chain (IL-10Rβ) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes
    • Kotenko, S. V., L. S. Izotova, O. V. Mirochnitchenko, E. Esterova, H. Dickensheets, R. P. Donnelly, and S. Petska. 2001. Identification of the functional interleukin-22 (IL-22) receptor complex: the IL-10R2 chain (IL-10Rβ) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes. J. Biol. Chem. 276:2725-2732.
    • (2001) J. Biol. Chem , vol.276 , pp. 2725-2732
    • Kotenko, S.V.1    Izotova, L.S.2    Mirochnitchenko, O.V.3    Esterova, E.4    Dickensheets, H.5    Donnelly, R.P.6    Petska, S.7
  • 14
    • 0034613201 scopus 로고    scopus 로고
    • Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R
    • Xie, M. H., S. Aggarwal, W. H. Ho, J. Foster, Z. Zhang, J. Stinson, W. I. Wood, A. D. Goddard, and A. L. Gurney. 2000. Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R. J. Biol. Chem. 275:31335-31339.
    • (2000) J. Biol. Chem , vol.275 , pp. 31335-31339
    • Xie, M.H.1    Aggarwal, S.2    Ho, W.H.3    Foster, J.4    Zhang, Z.5    Stinson, J.6    Wood, W.I.7    Goddard, A.D.8    Gurney, A.L.9
  • 15
    • 2142653517 scopus 로고    scopus 로고
    • Expression patterns of IL-10 ligand and receptor gene families provide leads for biological characterization
    • Nagalakshmi, M. L., E. Murphy, T. McClanahan, and R. de Waal Malefyt. 2004. Expression patterns of IL-10 ligand and receptor gene families provide leads for biological characterization. Int. Immuno-pharmacol. 4:577-592.
    • (2004) Int. Immuno-pharmacol , vol.4 , pp. 577-592
    • Nagalakshmi, M.L.1    Murphy, E.2    McClanahan, T.3    de Waal Malefyt, R.4
  • 19
    • 4344581122 scopus 로고    scopus 로고
    • The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation
    • Logsdon, N. J., B. C. Jones, J. C. Allman, L. Izotova, B. Schwartz, S. Pestka, and M. R. Walter. 2004. The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation. J. Mol. Biol. 342:503-514.
    • (2004) J. Mol. Biol , vol.342 , pp. 503-514
    • Logsdon, N.J.1    Jones, B.C.2    Allman, J.C.3    Izotova, L.4    Schwartz, B.5    Pestka, S.6    Walter, M.R.7
  • 22
    • 0029995691 scopus 로고    scopus 로고
    • Crystal structure of human interleukin-10 at 1.6 Å resolution and a model of a complex with its soluble receptor
    • Zdanov, A., C. Schalk-Hihi, and A. Wlodawer. 1996. Crystal structure of human interleukin-10 at 1.6 Å resolution and a model of a complex with its soluble receptor. Protein Sci. 5:1955-1962.
    • (1996) Protein Sci , vol.5 , pp. 1955-1962
    • Zdanov, A.1    Schalk-Hihi, C.2    Wlodawer, A.3
  • 23
    • 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
  • 25
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch, M. H., P. Vachette, and D. I. Svergun. 2003. Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q. Rev. Biophys. 36:147-227.
    • (2003) Q. Rev. Biophys , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 26
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • Svergun, D. I., and M. H. Koch. 2003. Small-angle scattering studies of biological macromolecules in solution. Rep. Prog. Phys. 66:1735-1782.
    • (2003) Rep. Prog. Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.2
  • 27
    • 0035877222 scopus 로고    scopus 로고
    • Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22
    • Dumoutier, L., D. Lejeune, D. Colau, and J. C. Renauld. 2001. Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22. J. Immunol. 166:7090-7095.
    • (2001) J. Immunol , vol.166 , pp. 7090-7095
    • Dumoutier, L.1    Lejeune, D.2    Colau, D.3    Renauld, J.C.4
  • 30
  • 33
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and K. Henrick. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60:2256-2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre, J., M. L. Huertas, and B. Carrasco. 2000. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78:719-730.
    • (2000) Biophys. J , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 38
    • 0029148581 scopus 로고
    • Crystal structure of inter-leukin 10 reveals an interferon γ-like fold
    • Walter, M. R., and T. L. Nagabhushan. 1995. Crystal structure of inter-leukin 10 reveals an interferon γ-like fold. Biochemistry. 34:12118-12125.
    • (1995) Biochemistry , vol.34 , pp. 12118-12125
    • Walter, M.R.1    Nagabhushan, T.L.2
  • 40
  • 41
    • 2342565785 scopus 로고    scopus 로고
    • Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases
    • Ceccarelli, E. A., A. K. Arakaki, N. Cortez, and N. Carrillo. 2004. Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases. Biochim. Biophys. Acta. 1698:155-165.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 155-165
    • Ceccarelli, E.A.1    Arakaki, A.K.2    Cortez, N.3    Carrillo, N.4
  • 42
    • 0014669944 scopus 로고
    • The modification of yeast hexokinases by proteases and its relationship to the dissociation of hexokinase into subunits
    • Schulze, I. T., and S. P. Colowick. 1969. The modification of yeast hexokinases by proteases and its relationship to the dissociation of hexokinase into subunits. J. Biol. Chem. 244:2306-2316.
    • (1969) J. Biol. Chem , vol.244 , pp. 2306-2316
    • Schulze, I.T.1    Colowick, S.P.2
  • 43
    • 0026743039 scopus 로고
    • Kinetics of the monomer-dimer reaction of yeast hexokinase PI
    • Hoggett, J. G., and G. L. Kellett. 1992. Kinetics of the monomer-dimer reaction of yeast hexokinase PI. Biochem. J. 287:567-572.
    • (1992) Biochem. J , vol.287 , pp. 567-572
    • Hoggett, J.G.1    Kellett, G.L.2
  • 44
    • 4243120936 scopus 로고    scopus 로고
    • Invited review: β-lactoglobulin: binding properties, structure, and function
    • Kontopidis, G., C. Holt, and L. Sawyer. 2004. Invited review: β-lactoglobulin: binding properties, structure, and function. J. Dairy Sci. 87:785-796.
    • (2004) J. Dairy Sci , vol.87 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 45
    • 0019133627 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 Å resolution
    • Bennett, W. S., Jr., and T. A. Steitz. 1980. Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 Å resolution. J. Mol. Biol. 140:183-209.
    • (1980) J. Mol. Biol , vol.140 , pp. 183-209
    • Bennett Jr., W.S.1    Steitz, T.A.2
  • 46
    • 0034617194 scopus 로고    scopus 로고
    • The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into its mechanism of action
    • Kuser, P. R., S. Krauchenco, O. A. Antunes, and I. Polikarpov. 2000. The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into its mechanism of action. J. Biol. Chem. 275:20814-20821.
    • (2000) J. Biol. Chem , vol.275 , pp. 20814-20821
    • Kuser, P.R.1    Krauchenco, S.2    Antunes, O.A.3    Polikarpov, I.4
  • 48
    • 0034825616 scopus 로고    scopus 로고
    • Crystal structures of bovine ß-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition
    • Oliveira, K. M., V. L. Valente-Mesquita, M. M. Botelho, L. Sawyer, S. T. Ferreira, and I. Polikarpov. 2001. Crystal structures of bovine ß-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition. Eur. J. Biochem. 268:477-483.
    • (2001) Eur. J. Biochem , vol.268 , pp. 477-483
    • Oliveira, K.M.1    Valente-Mesquita, V.L.2    Botelho, M.M.3    Sawyer, L.4    Ferreira, S.T.5    Polikarpov, I.6
  • 49
    • 33845948477 scopus 로고    scopus 로고
    • Conformational changes mediate IL-10R2 binding to IL-10 and assembly of the signaling complex
    • Yoon, S. I., N. J. Logsdon, F. Sheikh, R. P. Donnelly, and M. R. Walter. 2006. Conformational changes mediate IL-10R2 binding to IL-10 and assembly of the signaling complex. J. Biol. Chem. 281:35088-35096.
    • (2006) J. Biol. Chem , vol.281 , pp. 35088-35096
    • Yoon, S.I.1    Logsdon, N.J.2    Sheikh, F.3    Donnelly, R.P.4    Walter, M.R.5
  • 52
    • 0028887017 scopus 로고
    • Role of ligand in retinoid signaling. 9-cis-retinoic acid modulates the oligomeric state of the retinoid X receptor
    • Kersten, S., L. Pan, P. Chambon, H. Gronemeyer, and N. Noy. 1995. Role of ligand in retinoid signaling. 9-cis-retinoic acid modulates the oligomeric state of the retinoid X receptor. Biochemistry. 34:13717-13721.
    • (1995) Biochemistry , vol.34 , pp. 13717-13721
    • Kersten, S.1    Pan, L.2    Chambon, P.3    Gronemeyer, H.4    Noy, N.5
  • 56
    • 33646552450 scopus 로고    scopus 로고
    • IL-22 regulates the expression of genes responsible for antimicrobial defense, cellular differentiation, and mobility in keratinocytes: A potential role in psoriasis
    • Wolk, K., E. Witte, E. Wallace, W. D. Docke, S. Kunz, K. Asadullah, H. D. Volk, W. Sterry, and R. Sabat. 2006. IL-22 regulates the expression of genes responsible for antimicrobial defense, cellular differentiation, and mobility in keratinocytes: a potential role in psoriasis. Eur. J. Immunol. 36:1309-1323.
    • (2006) Eur. J. Immunol , vol.36 , pp. 1309-1323
    • Wolk, K.1    Witte, E.2    Wallace, E.3    Docke, W.D.4    Kunz, S.5    Asadullah, K.6    Volk, H.D.7    Sterry, W.8    Sabat, R.9
  • 58
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan, Q. R., and W. A. Hendrickson. 2005. Structure of human follicle-stimulating hormone in complex with its receptor. Nature. 433:269-277.
    • (2005) Nature , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.