메뉴 건너뛰기




Volumn 4, Issue 12, 2003, Pages 1213-1222

Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2Kb

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE;

EID: 0347382594     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/ni1006     Document Type: Article
Times cited : (115)

References (50)
  • 1
    • 0036774998 scopus 로고    scopus 로고
    • Variable receptors controlling activation and inhibition of NK cells
    • McQueen, K.L. & Parham, P. Variable receptors controlling activation and inhibition of NK cells. Curr. Opin. Immunol. 14, 615-621 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 615-621
    • McQueen, K.L.1    Parham, P.2
  • 2
    • 0038316337 scopus 로고    scopus 로고
    • Immune functions encoded by the natural killer gene complex
    • Plougastel, B.F.M. & Yokoyama, W.M. Immune functions encoded by the natural killer gene complex. Nat. Rev. Immunol. 3, 304-316 (2003).
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 304-316
    • Plougastel, B.F.M.1    Yokoyama, W.M.2
  • 3
    • 0036214286 scopus 로고    scopus 로고
    • Structure and function of natural killer cell receptors: Multiple molecular solutions to self, non-self discrimination
    • Natarajan, K., Dimasi, N., Wang, J., Mariuzza, R.A. & Margulies, D.H. Structure and function of natural killer cell receptors: multiple molecular solutions to self, non-self discrimination. Annu. Rev. Immunol. 20, 853-885 (2002).
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 853-885
    • Natarajan, K.1    Dimasi, N.2    Wang, J.3    Mariuzza, R.A.4    Margulies, D.H.5
  • 4
    • 0036604988 scopus 로고    scopus 로고
    • Lymphocyte activation via NKG2D: Towards a new paradigm in immune recognition?
    • Vivier, E., Tomasello, E. & Paul, P. Lymphocyte activation via NKG2D: towards a new paradigm in immune recognition? Curr. Opin. Immunol. 14, 306-311 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 306-311
    • Vivier, E.1    Tomasello, E.2    Paul, P.3
  • 5
    • 0034900399 scopus 로고    scopus 로고
    • The ever-expanding Ly49 gene family: Repertoire and signaling
    • Anderson, S.K., Ortaldo, J.R. & McVicar, D.W. The ever-expanding Ly49 gene family: repertoire and signaling. Immunol. Rev. 181, 79-89 (2001).
    • (2001) Immunol. Rev. , vol.181 , pp. 79-89
    • Anderson, S.K.1    Ortaldo, J.R.2    McVicar, D.W.3
  • 6
    • 0037123607 scopus 로고    scopus 로고
    • Direct recognition of cytomegalovirus by activating and inhibitory NK cell receptors
    • Arase, H., Mocarski, E.S., Campbell, A.E., Hill, A.B. & Lanier, L.L. Direct recognition of cytomegalovirus by activating and inhibitory NK cell receptors. Science 296, 1323-1326 (2002).
    • (2002) Science , vol.296 , pp. 1323-1326
    • Arase, H.1    Mocarski, E.S.2    Campbell, A.E.3    Hill, A.B.4    Lanier, L.L.5
  • 7
    • 0037172968 scopus 로고    scopus 로고
    • Recognition of a virus-encoded ligand by a natural killer cell activation receptor
    • Smith, H.R. et al. Recognition of a virus-encoded ligand by a natural killer cell activation receptor. Proc. Natl. Acad. Sci. USA 99, 8826-8831 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8826-8831
    • Smith, H.R.1
  • 8
    • 17544396947 scopus 로고    scopus 로고
    • Peptide dependency and selectivity of the NK inhibitory receptor Ly-49C
    • Franksson, L. et al. Peptide dependency and selectivity of the NK inhibitory receptor Ly-49C. Eur. J. Immunol. 29, 2748-2758 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2748-2758
    • Franksson, L.1
  • 9
    • 0033166539 scopus 로고    scopus 로고
    • Direct assessment of MHC class I binding by seven Ly49 inhibitory NK cell receptors
    • Hanke, T. et al. Direct assessment of MHC class I binding by seven Ly49 inhibitory NK cell receptors. Immunity 11, 67-77 (1999).
    • (1999) Immunity , vol.11 , pp. 67-77
    • Hanke, T.1
  • 10
    • 0034909777 scopus 로고    scopus 로고
    • Structure of killer cell immunoglobulin-like receptors and their recognition of the class I MHC molecules
    • Boyington, J.C., Brooks, A.G. & Sun, P.D. Structure of killer cell immunoglobulin-like receptors and their recognition of the class I MHC molecules. Immunol. Rev. 181, 66-78 (2001).
    • (2001) Immunol. Rev. , vol.181 , pp. 66-78
    • Boyington, J.C.1    Brooks, A.G.2    Sun, P.D.3
  • 11
    • 0035347169 scopus 로고    scopus 로고
    • Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA
    • Li, P. et al. Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA. Nat. Immunol. 2, 443-451 (2001).
    • (2001) Nat. Immunol. , vol.2 , pp. 443-451
    • Li, P.1
  • 12
    • 0033540084 scopus 로고    scopus 로고
    • Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand
    • Tormo, J., Natarajan, K., Margulies, D.H. & Mariuzza, R.A. Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand. Nature 402, 623-631 (1999).
    • (1999) Nature , vol.402 , pp. 623-631
    • Tormo, J.1    Natarajan, K.2    Margulies, D.H.3    Mariuzza, R.A.4
  • 13
    • 0035862324 scopus 로고    scopus 로고
    • The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex class I ligand
    • Matsumoto, N., Mitsuki, M., Tajima, K., Yokoyama, W.M. & Yamamoto, K. The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex class I ligand. J. Exp. Med. 193, 147-158 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 147-158
    • Matsumoto, N.1    Mitsuki, M.2    Tajima, K.3    Yokoyama, W.M.4    Yamamoto, K.5
  • 14
    • 0037059744 scopus 로고    scopus 로고
    • 2-microglobulin
    • 2-microglobulin. J. Biol. Chem. 277, 1433-1442 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1433-1442
    • Wang, J.1
  • 15
    • 0032400976 scopus 로고    scopus 로고
    • External and internal calibration of the MHC class I-specific receptor Ly49A on murine natural killer cells
    • Kåse, A., Johansson, M.H., Olsson-Alheim, M.Y., Kärre, K. & Höglund, P. External and internal calibration of the MHC class I-specific receptor Ly49A on murine natural killer cells. J. Immunol. 161, 6133-6138 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 6133-6138
    • Kåse, A.1    Johansson, M.H.2    Olsson-Alheim, M.Y.3    Kärre, K.4    Höglund, P.5
  • 16
    • 0032534589 scopus 로고    scopus 로고
    • MHC class I mosaic mice reveal insights into control of Ly49C inhibitory receptor expression in NK cells
    • Andersson, M. et al. MHC class I mosaic mice reveal insights into control of Ly49C inhibitory receptor expression in NK cells. J. Immunol. 161, 6475-6479 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 6475-6479
    • Andersson, M.1
  • 17
    • 0035914743 scopus 로고    scopus 로고
    • + natural killer (NK) cells precludes ligand uptake from environmental cells
    • + natural killer (NK) cells precludes ligand uptake from environmental cells. J. Exp. Med. 194, 1531-1539 (2001).
    • (2001) J. Exp. Med. , vol.194 , pp. 1531-1539
    • Zimmer, J.1    Ionnidis, V.2    Held, W.3
  • 18
    • 0034671628 scopus 로고    scopus 로고
    • Mapping the ligand of the NK inhibitory receptor Ly49A on living cells
    • Chung, D.H. et al. Mapping the ligand of the NK inhibitory receptor Ly49A on living cells. J. Immunol. 165, 6922-6932 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 6922-6932
    • Chung, D.H.1
  • 19
    • 0033230387 scopus 로고    scopus 로고
    • d: Identification of a site distinct from the TCR site
    • d: identification of a site distinct from the TCR site. Immunity 11, 591-601 (1999).
    • (1999) Immunity , vol.11 , pp. 591-601
    • Natarajan, K.1
  • 20
    • 0037080044 scopus 로고    scopus 로고
    • NK cell inhibitory receptor Ly-49C residues involved in MHC class I binding
    • Sundbäck, J., Achour, A., Michaesson, J., Lindstrom, H. & Kärre, K. NK cell inhibitory receptor Ly-49C residues involved in MHC class I binding. J. Immunol. 168, 793-800 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 793-800
    • Sundbäck, J.1    Achour, A.2    Michaesson, J.3    Lindstrom, H.4    Kärre, K.5
  • 21
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder, E.T. & Wittrup, K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat, Biotech. 15, 553-557 (1997).
    • (1997) Nat. Biotech. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 22
    • 0033545862 scopus 로고    scopus 로고
    • Selection of functional T cell receptor mutants from a yeast surface-display library
    • Kieke, M.C. et al. Selection of functional T cell receptor mutants from a yeast surface-display library. Proc. Natl. Acad. Sci. USA 96, 5651-5656 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5651-5656
    • Kieke, M.C.1
  • 23
    • 0036311182 scopus 로고    scopus 로고
    • Crystal structure of the Ly491 natural killer cell receptor reveals variability in dimerization mode within the Ly49 family
    • Dimasi, N. et al. Crystal structure of the Ly491 natural killer cell receptor reveals variability in dimerization mode within the Ly49 family. J. Mol. Biol. 320, 573-585 (2002).
    • (2002) J. Mol. Biol. , vol.320 , pp. 573-585
    • Dimasi, N.1
  • 24
    • 0033536626 scopus 로고    scopus 로고
    • Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency
    • Shusta, E.V., Kieke, M.C., Parke, E., Kranz, D.M. & Wittrup, K.D. Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency. J. Mol. Biol. 292, 949-956 (1999).
    • (1999) J. Mol. Biol. , vol.292 , pp. 949-956
    • Shusta, E.V.1    Kieke, M.C.2    Parke, E.3    Kranz, D.M.4    Wittrup, K.D.5
  • 25
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre, J., Huertas, M.L. & Carrasco, B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 26
    • 0035693584 scopus 로고    scopus 로고
    • CD8 binding to MHC class I molecules is influenced by T cell maturation and glycosylation
    • Daniels, M.A. et al. CD8 binding to MHC class I molecules is influenced by T cell maturation and glycosylation. Immunity 15, 1051-1061 (2001).
    • (2001) Immunity , vol.15 , pp. 1051-1061
    • Daniels, M.A.1
  • 27
    • 0027772959 scopus 로고
    • Shape complementarity at protein-protein interfaces
    • Lawrence, M.C. & Colman, P.M. Shape complementarity at protein-protein interfaces. J. Mol. Biol. 234, 946-950 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 28
    • 0035286344 scopus 로고    scopus 로고
    • Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95 Å
    • Wolan, D.W. et al.Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95 Å. Nat. Immunol. 2, 248-254 (2001).
    • (2001) Nat. Immunol. , vol.2 , pp. 248-254
    • Wolan, D.W.1
  • 29
    • 0035695983 scopus 로고    scopus 로고
    • Conformational plasticity revealed by the co-crystal structure of the activating NK receptor NKG2D and its MHC-like ligand ULBP
    • Radaev, S., Rostro, B., Brooks, A.G., Colonna, M. & Sun, P. Conformational plasticity revealed by the co-crystal structure of the activating NK receptor NKG2D and its MHC-like ligand ULBP. Immunity 15, 1039-1049 (2001).
    • (2001) Immunity , vol.15 , pp. 1039-1049
    • Radaev, S.1    Rostro, B.2    Brooks, A.G.3    Colonna, M.4    Sun, P.5
  • 30
    • 0036467394 scopus 로고    scopus 로고
    • The specificity of TCR/pMHC interaction
    • Rudolph, M.G. & Wilson, I.A. The specificity of TCR/pMHC interaction. Curr. Opin. Immunol. 14, 52-65 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 52-65
    • Rudolph, M.G.1    Wilson, I.A.2
  • 31
    • 0036467503 scopus 로고    scopus 로고
    • So many ways of getting in the way: Diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes
    • Sundberg, E.J., Li, Y. & Mariuzza, R.A. So many ways of getting in the way: diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes. Curr. Opin. Immunol. 14, 36-44 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 36-44
    • Sundberg, E.J.1    Li, Y.2    Mariuzza, R.A.3
  • 33
    • 0028987213 scopus 로고
    • b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove
    • b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl. Acad. Sci. USA 92, 2479-2483 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2479-2483
    • Fremont, D.H.1    Stura, E.A.2    Matsumura, M.3    Peterson, P.A.4    Wilson, I.A.5
  • 34
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antigen-antibody complexes
    • Sundberg, E.J. & Mariuzza, R.A. Molecular recognition in antigen-antibody complexes. Adv. Protein Chem. 61, 119-160 (2002).
    • (2002) Adv. Protein Chem. , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 35
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden, D.R. The three-dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 13, 587-622 (1995).
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 36
    • 0030926140 scopus 로고    scopus 로고
    • Crystal structure of the complex between human CD8αα and HLA-A2
    • Gao, G.F. et al. Crystal structure of the complex between human CD8αα and HLA-A2. Nature 387, 630-634 (1997).
    • (1997) Nature , vol.387 , pp. 630-634
    • Gao, G.F.1
  • 39
    • 0035896394 scopus 로고    scopus 로고
    • Structure of an extracellular gp130 cytokine receptor signaling complex
    • Chow, D., He, X., Snow, A.L., Rose-John, S. & Garcia, K.C. Structure of an extracellular gp130 cytokine receptor signaling complex. Science 291, 2150-2155 (2001).
    • (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
  • 40
    • 0030926137 scopus 로고    scopus 로고
    • Ligand-specific oligomerization of T-cell receptor molecules
    • Reich, Z. et al. Ligand-specific oligomerization of T-cell receptor molecules. Nature 387, 617-620 (1997).
    • (1997) Nature , vol.387 , pp. 617-620
    • Reich, Z.1
  • 41
    • 0033082989 scopus 로고    scopus 로고
    • Qualitative and quantitative differences in T cell receptor binding of agonist and antagonist ligands
    • Alam, S.M. et al. Qualitative and quantitative differences in T cell receptor binding of agonist and antagonist ligands. Immunity 10, 227-237 (1999).
    • (1999) Immunity , vol.10 , pp. 227-237
    • Alam, S.M.1
  • 42
    • 0029071074 scopus 로고
    • Oligomerization of CD4 is required for stable binding to class II major histocompatibility complex proteins but not for interaction with human immunodeficiency virus gp120
    • Sakihama, T., Smolyar, A. & Reinherz, E.L. Oligomerization of CD4 is required for stable binding to class II major histocompatibility complex proteins but not for interaction with human immunodeficiency virus gp120. Proc. Natl. Acad. Sci. USA 92, 6444-6448 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6444-6448
    • Sakihama, T.1    Smolyar, A.2    Reinherz, E.L.3
  • 43
    • 0030911709 scopus 로고    scopus 로고
    • Dimeric association and segmental variability in the structure of CD4
    • Wu, H., Kwong, P.D. & Hendrickson, W.A. Dimeric association and segmental variability in the structure of CD4. Nature 387, 527-530 (1997).
    • (1997) Nature , vol.387 , pp. 527-530
    • Wu, H.1    Kwong, P.D.2    Hendrickson, W.A.3
  • 44
    • 0034948340 scopus 로고    scopus 로고
    • αβ T cell receptor ligand-specific oligomerization revisited
    • Baker, B.M. & Wiley, D.C. αβ T cell receptor ligand-specific oligomerization revisited. Immunity 14, 681-692 (2001).
    • (2001) Immunity , vol.14 , pp. 681-692
    • Baker, B.M.1    Wiley, D.C.2
  • 45
    • 0035845583 scopus 로고    scopus 로고
    • Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule
    • Wang, J.H. et al. Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule. Proc. Natl. Acad. Sci. USA 98, 10799-10804 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10799-10804
    • Wang, J.H.1
  • 46
    • 0037331525 scopus 로고    scopus 로고
    • Quantitative analysis of the contribution of TCR/pepMHC affinity and CD8 to T cell activation
    • Holler, P.D. & Kranz, D.M. Quantitative analysis of the contribution of TCR/pepMHC affinity and CD8 to T cell activation. Immunity 18, 255-264 (2003).
    • (2003) Immunity , vol.18 , pp. 255-264
    • Holler, P.D.1    Kranz, D.M.2
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 49
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 50
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit. A versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E. XtalView/Xfit. A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.