메뉴 건너뛰기




Volumn 400, Issue 4, 2010, Pages 838-846

Crystal structure of mouse MD-1 with endogenous phospholipid bound in its cavity

Author keywords

Crystal structure; Glycoprotein; LPS; MD 1; MD 2 related lipid recognition protein

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN MD 1; GLYCOPROTEIN MD 2; OLIGOMER; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 77954384339     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.05.063     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0032146713 scopus 로고    scopus 로고
    • Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression
    • Miyake K., Shimazu R., Kondo J., Niki T., Akashi S., Ogata H., et al. Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression. J. Immunol. 1998, 161:1348-1353.
    • (1998) J. Immunol. , vol.161 , pp. 1348-1353
    • Miyake, K.1    Shimazu, R.2    Kondo, J.3    Niki, T.4    Akashi, S.5    Ogata, H.6
  • 2
    • 0036558018 scopus 로고    scopus 로고
    • ML-a conserved domain involved in innate immunity and lipid metabolism
    • Inohara N., Nunez G. ML-a conserved domain involved in innate immunity and lipid metabolism. Trends Biochem. Sci. 2002, 27:219-221.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 219-221
    • Inohara, N.1    Nunez, G.2
  • 4
    • 34548459868 scopus 로고    scopus 로고
    • Structure and function of Toll receptors and their ligands
    • Gay N.J., Gangloff M. Structure and function of Toll receptors and their ligands. Annu. Rev. Biochem. 2007, 76:141-165.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 141-165
    • Gay, N.J.1    Gangloff, M.2
  • 5
    • 0034958947 scopus 로고    scopus 로고
    • Epidemiology of severe sepsis in the United States: analysis of incidence, outcome, and associated costs of care
    • Angus D.C., Linde-Zwirble W.T., Lidicker J., Clermont G., Carcillo J., Pinsky M.R. Epidemiology of severe sepsis in the United States: analysis of incidence, outcome, and associated costs of care. Crit. Care Med. 2001, 29:1303-1310.
    • (2001) Crit. Care Med. , vol.29 , pp. 1303-1310
    • Angus, D.C.1    Linde-Zwirble, W.T.2    Lidicker, J.3    Clermont, G.4    Carcillo, J.5    Pinsky, M.R.6
  • 6
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu R., Akashi S., Ogata H., Nagai Y., Fukudome K., Miyake K., Kimoto M. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 1999, 189:1777-1782.
    • (1999) J. Exp. Med. , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6    Kimoto, M.7
  • 7
    • 0028071612 scopus 로고
    • Murine B-cell proliferation and protection from apoptosis with an antibody against a 105-kDa molecule-unresponsiveness of X-linked immunodeficient B-cells
    • Miyake K., Yamashita Y., Hitoshi Y., Takatsu K., Kimoto M. Murine B-cell proliferation and protection from apoptosis with an antibody against a 105-kDa molecule-unresponsiveness of X-linked immunodeficient B-cells. J. Exp. Med. 1994, 180:1217-1224.
    • (1994) J. Exp. Med. , vol.180 , pp. 1217-1224
    • Miyake, K.1    Yamashita, Y.2    Hitoshi, Y.3    Takatsu, K.4    Kimoto, M.5
  • 8
    • 0028949390 scopus 로고
    • RP105, a novel B-cell surface-molecule implicated in B-cell activation, is a member of the leucine-rich repeat protein family
    • Miyake K., Yamashita Y., Ogata M., Sudo T., Kimoto M. RP105, a novel B-cell surface-molecule implicated in B-cell activation, is a member of the leucine-rich repeat protein family. J. Immunol. 1995, 154:3333-3340.
    • (1995) J. Immunol. , vol.154 , pp. 3333-3340
    • Miyake, K.1    Yamashita, Y.2    Ogata, M.3    Sudo, T.4    Kimoto, M.5
  • 9
    • 0036493503 scopus 로고    scopus 로고
    • Requirement for MD-1 in cell surface expression of RP105/CD180 and B-cell responsiveness to lipopolysaccharide
    • Nagai Y., Shimazu R., Ogata H., Akashi S., Sudo K., Yamasaki H., et al. Requirement for MD-1 in cell surface expression of RP105/CD180 and B-cell responsiveness to lipopolysaccharide. Blood 2002, 99:1699-1705.
    • (2002) Blood , vol.99 , pp. 1699-1705
    • Nagai, Y.1    Shimazu, R.2    Ogata, H.3    Akashi, S.4    Sudo, K.5    Yamasaki, H.6
  • 10
    • 0034601022 scopus 로고    scopus 로고
    • The toll-like receptor protein RP105 regulates lipopolysaccharide signaling in B cells
    • Ogata H., Su I., Miyake K., Nagai Y., Akashi S., Mecklenbrauker I., et al. The toll-like receptor protein RP105 regulates lipopolysaccharide signaling in B cells. J. Exp. Med. 2000, 192:23-29.
    • (2000) J. Exp. Med. , vol.192 , pp. 23-29
    • Ogata, H.1    Su, I.2    Miyake, K.3    Nagai, Y.4    Akashi, S.5    Mecklenbrauker, I.6
  • 11
    • 20644450101 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105
    • Divanovic S., Trompette A., Atabani S.F., Madan R., Golenbock D.T., Visintin A., et al. Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105. Nat. Immunol. 2005, 6:571-578.
    • (2005) Nat. Immunol. , vol.6 , pp. 571-578
    • Divanovic, S.1    Trompette, A.2    Atabani, S.F.3    Madan, R.4    Golenbock, D.T.5    Visintin, A.6
  • 12
    • 0033513310 scopus 로고    scopus 로고
    • B cells lacking RP105, a novel B cell antigen, in systemic lupus erythematosus
    • Koarada S., Tada Y., Ushiyama O., Morito F., Suzuki N., Ohta A., et al. B cells lacking RP105, a novel B cell antigen, in systemic lupus erythematosus. Arthritis Rheum. 1999, 42:2593-2600.
    • (1999) Arthritis Rheum. , vol.42 , pp. 2593-2600
    • Koarada, S.1    Tada, Y.2    Ushiyama, O.3    Morito, F.4    Suzuki, N.5    Ohta, A.6
  • 13
    • 34250813748 scopus 로고    scopus 로고
    • Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa
    • Ohto U., Fukase K., Miyake K., Satow Y. Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa. Science 2007, 316:1632-1634.
    • (2007) Science , vol.316 , pp. 1632-1634
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Satow, Y.4
  • 14
    • 34548222514 scopus 로고    scopus 로고
    • Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist eritoran
    • Kim H.M., Park B.S., Kim J.I., Kim S.E., Lee J., Oh S.C., et al. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist eritoran. Cell 2007, 130:906-917.
    • (2007) Cell , vol.130 , pp. 906-917
    • Kim, H.M.1    Park, B.S.2    Kim, J.I.3    Kim, S.E.4    Lee, J.5    Oh, S.C.6
  • 15
    • 0346850824 scopus 로고    scopus 로고
    • Lysines 128 and 132 enable lipopolysaccharide binding to MD-2, leading to Toll-like receptor-4 aggregation and signal transduction
    • Visintin A., Latz E., Monks B.G., Espevik T., Golenbock D.T. Lysines 128 and 132 enable lipopolysaccharide binding to MD-2, leading to Toll-like receptor-4 aggregation and signal transduction. J. Biol. Chem. 2003, 278:48313-48320.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48313-48320
    • Visintin, A.1    Latz, E.2    Monks, B.G.3    Espevik, T.4    Golenbock, D.T.5
  • 16
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park B.S., Song D.H., Kim H.M., Choi B.S., Lee H., Lee J.O. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 2009, 458:1191-1195.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5    Lee, J.O.6
  • 17
    • 0027968068 scopus 로고
    • CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 18
    • 0026632806 scopus 로고
    • Biological activity of synthetic phosphonooxyethyl analogs of lipid A and lipid A partial structures
    • Ulmer A.J., Heine H., Feist W., Kusumoto S., Kusama T., Brade H., et al. Biological activity of synthetic phosphonooxyethyl analogs of lipid A and lipid A partial structures. Infect. Immun. 1992, 60:3309-3314.
    • (1992) Infect. Immun. , vol.60 , pp. 3309-3314
    • Ulmer, A.J.1    Heine, H.2    Feist, W.3    Kusumoto, S.4    Kusama, T.5    Brade, H.6
  • 19
    • 0347659154 scopus 로고    scopus 로고
    • Structural basis for endotoxic and antagonistic activities: investigation with novel synthetic lipid A analogs
    • Kusumoto S., Fukase K., Fukase Y., Kataoka M., Yoshizaki H., Sato K., et al. Structural basis for endotoxic and antagonistic activities: investigation with novel synthetic lipid A analogs. J. Endotoxin Res. 2003, 9:361-366.
    • (2003) J. Endotoxin Res. , vol.9 , pp. 361-366
    • Kusumoto, S.1    Fukase, K.2    Fukase, Y.3    Kataoka, M.4    Yoshizaki, H.5    Sato, K.6
  • 22
    • 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. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0028103275 scopus 로고
    • The CCP4 Suite: programs for protein crystallography
    • Collaborative Computational Project, No.4
    • Collaborative Computational Project, No.4 The CCP4 Suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50:760-763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 29
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design
    • Liang J., Edelsbrunner H., Woodward C. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 1998, 7:1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.