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Volumn 288, Issue 27, 2013, Pages 19528-19536

Dynamics of the antigen-binding grooves in CD1 proteins: Reversible hydrophobic collapse in the lipid-free state

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN-BINDING; CELLULAR INTERNALIZATION; HYDROPHOBIC CAVITIES; HYDROPHOBIC COLLAPSE; INTRACELLULAR PATHWAYS; LIPID TRANSFER PROTEIN; MOLECULAR DYNAMICS SIMULATIONS; STRUCTURAL FEATURE;

EID: 84880070645     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.470179     Document Type: Article
Times cited : (16)

References (51)
  • 3
    • 36448952375 scopus 로고    scopus 로고
    • CD1 antigen presentation. How it works
    • Barral, D. C., and Brenner, M. B. (2007) CD1 antigen presentation. How it works. Nat. Rev. Immunol. 7, 929-941
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 929-941
    • Barral, D.C.1    Brenner, M.B.2
  • 6
    • 77249151524 scopus 로고    scopus 로고
    • Recent advances in processing and presentation of CD1 bound lipid antigens
    • Salio, M., Silk, J. D., and Cerundolo, V. (2010) Recent advances in processing and presentation of CD1 bound lipid antigens. Curr. Opin. Immunol. 22, 81-88
    • (2010) Curr. Opin. Immunol , vol.22 , pp. 81-88
    • Salio, M.1    Silk, J.D.2    Cerundolo, V.3
  • 7
    • 84857684717 scopus 로고    scopus 로고
    • Novel insights into lipid antigen presentation
    • De Libero, G., and Mori, L. (2012) Novel insights into lipid antigen presentation. Trends Immunol. 33, 103-111
    • (2012) Trends Immunol , vol.33 , pp. 103-111
    • De Libero, G.1    Mori, L.2
  • 8
    • 0030826423 scopus 로고    scopus 로고
    • Crystal structure of mouse CD1. An MHC-like fold with a large hydrophobic binding groove
    • Zeng, Z., Castaño, A. R., Segelke, B. W., Stura, E. A., Peterson, P. A., and Wilson, I. A. (1997) Crystal structure of mouse CD1. An MHC-like fold with a large hydrophobic binding groove. Science 277, 339-345
    • (1997) Science , vol.277 , pp. 339-345
    • Zeng, Z.1    Castaño, A.R.2    Segelke, B.W.3    Stura, E.A.4    Peterson, P.A.5    Wilson, I.A.6
  • 10
    • 0043198070 scopus 로고    scopus 로고
    • Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 Å
    • Zajonc, D. M., Elsliger, M. A., Teyton, L., and Wilson, I. A. (2003) Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 Å. Nat. Immunol. 4, 808-815
    • (2003) Nat. Immunol , vol.4 , pp. 808-815
    • Zajonc, D.M.1    Elsliger, M.A.2    Teyton, L.3    Wilson, I.A.4
  • 13
    • 28544442722 scopus 로고    scopus 로고
    • Structural basis for CD1d presentation of a sulfatide derived from myelin and its implications for autoimmunity
    • Zajonc, D. M., Maricic, I., Wu, D., Halder, R., Roy, K., Wong, C. H., Kumar, V., and Wilson, I. A. (2005) Structural basis for CD1d presentation of a sulfatide derived from myelin and its implications for autoimmunity. J. Exp. Med. 202, 1517-1526
    • (2005) J. Exp. Med , vol.202 , pp. 1517-1526
    • Zajonc, D.M.1    Maricic, I.2    Wu, D.3    Halder, R.4    Roy, K.5    Wong, C.H.6    Kumar, V.7    Wilson, I.A.8
  • 15
    • 56649109840 scopus 로고    scopus 로고
    • The crystal structure of avian CD1 reveals a smaller, more primordial antigenbinding pocket compared to mammalian CD1
    • Zajonc, D. M., Striegl, H., Dascher, C. C., and Wilson, I. A. (2008) The crystal structure of avian CD1 reveals a smaller, more primordial antigenbinding pocket compared to mammalian CD1. Proc. Natl. Acad. Sci. U.S.A. 105, 17925-17930
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 17925-17930
    • Zajonc, D.M.1    Striegl, H.2    Dascher, C.C.3    Wilson, I.A.4
  • 19
    • 70450224660 scopus 로고    scopus 로고
    • Predicted structural basis for CD1c presentation of mycobacterial branched polyketides and long lipopeptide antigens
    • Garzón, D., Bond, P. J., and Faraldo-Gómez, J. D. (2009) Predicted structural basis for CD1c presentation of mycobacterial branched polyketides and long lipopeptide antigens. Mol. Immunol. 47, 253-260
    • (2009) Mol. Immunol , vol.47 , pp. 253-260
    • Garzón, D.1    Bond, P.J.2    Faraldo-Gómez, J.D.3
  • 20
    • 0035690582 scopus 로고    scopus 로고
    • CD1 trafficking: Invariant chain gives a new twist to the tale
    • Moody, D. B., and Porcelli, S. A. (2001) CD1 trafficking: invariant chain gives a new twist to the tale. Immunity 15, 861-865
    • (2001) Immunity , vol.15 , pp. 861-865
    • Moody, D.B.1    Porcelli, S.A.2
  • 21
    • 0037084102 scopus 로고    scopus 로고
    • Intracellular trafficking pathway of newly synthesized CD1b molecules
    • Briken, V., Jackman, R. M., Dasgupta, S., Hoening, S., and Porcelli, S. A. (2002) Intracellular trafficking pathway of newly synthesized CD1b molecules. EMBO J. 21, 825-834
    • (2002) EMBO J. , vol.21 , pp. 825-834
    • Briken, V.1    Jackman, R.M.2    Dasgupta, S.3    Hoening, S.4    Porcelli, S.A.5
  • 22
    • 20644445206 scopus 로고    scopus 로고
    • Recognition of lipid antigens by T cells
    • De Libero, G., and Mori, L. (2005) Recognition of lipid antigens by T cells. Nat. Rev. Immunol. 5, 485-496
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 485-496
    • De Libero, G.1    Mori, L.2
  • 23
    • 0028970661 scopus 로고
    • TAP-independent, β 2-microglobulin-dependent surface expression of functional mouse CD1.1
    • Brutkiewicz, R. R., Bennink, J. R., Yewdell, J. W., and Bendelac, A. (1995) TAP-independent, β 2-microglobulin-dependent surface expression of functional mouse CD1.1. J. Exp. Med. 182, 1913-1919
    • (1995) J. Exp. Med , vol.182 , pp. 1913-1919
    • Brutkiewicz, R.R.1    Bennink, J.R.2    Yewdell, J.W.3    Bendelac, A.4
  • 25
    • 0031227791 scopus 로고    scopus 로고
    • Assembly and retention of CD1b heavy chains in the endoplasmic reticulum
    • Sugita, M., Porcelli, S. A., and Brenner, M. B. (1997) Assembly and retention of CD1b heavy chains in the endoplasmic reticulum. J. Immunol. 159, 2358-2365
    • (1997) J. Immunol , vol.159 , pp. 2358-2365
    • Sugita, M.1    Porcelli, S.A.2    Brenner, M.B.3
  • 26
    • 0345425612 scopus 로고    scopus 로고
    • Analysis of the early biogenesis of CD1b Involvement of the chaperones calnexin and calreticulin, the proteasome and β(2)-microglobulin
    • Hüttinger, R., Staffler, G., Majdic, O., and Stockinger, H. (1999) Analysis of the early biogenesis of CD1b. Involvement of the chaperones calnexin and calreticulin, the proteasome and β(2)-microglobulin. Int. Immunol. 11, 1615-1623
    • (1999) Int. Immunol , vol.11 , pp. 1615-1623
    • Hüttinger, R.1    Staffler, G.2    Majdic, O.3    Stockinger, H.4
  • 27
    • 0037160108 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain
    • Kang, S. J., and Cresswell, P. (2002) Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain. J. Biol. Chem. 277, 44838-44844
    • (2002) J. Biol. Chem , vol.277 , pp. 44838-44844
    • Kang, S.J.1    Cresswell, P.2
  • 29
    • 0034172885 scopus 로고    scopus 로고
    • Pathways for lipid antigen presentation by CD1 molecules. Nowhere for intracellular pathogens to hide
    • Sugita, M., Peters, P. J., and Brenner, M. B. (2000) Pathways for lipid antigen presentation by CD1 molecules. Nowhere for intracellular pathogens to hide. Traffic 1, 295-300
    • (2000) Traffic , vol.1 , pp. 295-300
    • Sugita, M.1    Peters, P.J.2    Brenner, M.B.3
  • 31
    • 1042278901 scopus 로고    scopus 로고
    • New insights into pathways for CD1-mediated antigen presentation
    • Sugita, M., Cernadas, M., and Brenner, M. B. (2004) New insights into pathways for CD1-mediated antigen presentation. Curr. Opin. Immunol. 16, 90-95
    • (2004) Curr. Opin. Immunol , vol.16 , pp. 90-95
    • Sugita, M.1    Cernadas, M.2    Brenner, M.B.3
  • 32
    • 77949324059 scopus 로고    scopus 로고
    • Early recycling compartment trafficking of CD1a is essential for its intersection and presentation of lipid antigens
    • Cernadas, M., Cavallari, M., Watts, G., Mori, L., De Libero, G., and Brenner, M. B. (2010) Early recycling compartment trafficking of CD1a is essential for its intersection and presentation of lipid antigens. J. Immunol. 184, 1235-1241
    • (2010) J. Immunol , vol.184 , pp. 1235-1241
    • Cernadas, M.1    Cavallari, M.2    Watts, G.3    Mori, L.4    De Libero, G.5    Brenner, M.B.6
  • 33
    • 1142263116 scopus 로고    scopus 로고
    • Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells
    • Kang, S. J., and Cresswell, P. (2004) Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells. Nat. Immunol. 5, 175-181
    • (2004) Nat. Immunol , vol.5 , pp. 175-181
    • Kang, S.J.1    Cresswell, P.2
  • 42
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4 Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., Van der Spoel, D., and Lindahl, E. (2008)GROMACS 4. Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 43
    • 0030844208 scopus 로고    scopus 로고
    • Molecular dynamics simulation of unsaturated lipid bilayers at low hydration: Parameterization and comparison with diffraction studies
    • Feller, S. E., Yin, D., Pastor, R. W., and MacKerell, A. D., Jr. (1997) Molecular dynamics simulation of unsaturated lipid bilayers at low hydration: parameterization and comparison with diffraction studies. Biophys. J. 73, 2269-2279
    • (1997) Biophys. J. , vol.73 , pp. 2269-2279
    • Feller, S.E.1    Yin, D.2    Pastor, R.W.3    MacKerell Jr., A.D.4
  • 46
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G. A., Friesner, R. A., Tirado-Rives, J., and Jorgensen, W. L. (2001) Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B 105, 6474-6487
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 49
    • 33846550599 scopus 로고    scopus 로고
    • Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class i alleles
    • Sieker, F., Springer, S., and Zacharias, M. (2007) Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class I alleles. Protein Sci. 16, 299-308
    • (2007) Protein Sci , vol.16 , pp. 299-308
    • Sieker, F.1    Springer, S.2    Zacharias, M.3
  • 50
    • 48049122834 scopus 로고    scopus 로고
    • Differential tapasin dependence of MHC class i molecules correlates with conformational changes upon peptide dissociation. A molecular dynamics simulation study
    • Sieker, F., Straatsma, T. P., Springer, S., and Zacharias, M. (2008) Differential tapasin dependence of MHC class I molecules correlates with conformational changes upon peptide dissociation. A molecular dynamics simulation study. Mol. Immunol. 45, 3714-3722
    • (2008) Mol. Immunol , vol.45 , pp. 3714-3722
    • Sieker, F.1    Straatsma, T.P.2    Springer, S.3    Zacharias, M.4


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