메뉴 건너뛰기




Volumn 7, Issue 3, 1999, Pages 255-264

Crystal structure of the trimeric α-helical coiled-coil and the three lectin domains of human lung surfactant protein D

Author keywords

C type lectin; CRD; Lung surfactant, SP D; Three dimensional structure

Indexed keywords

CARBOHYDRATE; LECTIN; LIPOPOLYSACCHARIDE; LUNG SURFACTANT; MANNAN; SURFACTANT PROTEIN D;

EID: 0033103527     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80036-7     Document Type: Article
Times cited : (128)

References (40)
  • 1
    • 0027293871 scopus 로고    scopus 로고
    • 2+-dependent carbohydrate-recognition domains in animal proteins
    • 2+-dependent carbohydrate-recognition domains in animal proteins. Curr. Opin. Struct. Biol. 3, 393-400.
    • (1998) Curr. Opin. Struct. Biol. , vol.3 , pp. 393-400
    • Drickamer, K.1
  • 2
    • 0027227391 scopus 로고
    • Structural similarity between lung surfactant protein D and conglutinin. Two distinct, C-type lectins containing collagen-like sequences
    • Lu, J., Wiedemann, H., Holmskov, U., Thiel, S., Timpl, R. & Reid, K.B.M. (1993). Structural similarity between lung surfactant protein D and conglutinin. Two distinct, C-type lectins containing collagen-like sequences. Eur. J. Biochem. 215, 793-799.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 793-799
    • Lu, J.1    Wiedemann, H.2    Holmskov, U.3    Thiel, S.4    Timpl, R.5    Reid, K.B.M.6
  • 3
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis, W.I., Kahn, R., Fourme, R., Drickamer, K. & Hendrickson, W.A. (1991 ). Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 254, 1608-1615.
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 4
    • 0028533911 scopus 로고
    • Human mannose- binding protein carbohydrate-recognition domain trimerizes through a triple α-helical coiled-coil
    • Sheriff, S., Chang, C.Y. & Ezekowitz, R.A.B. (1994). Human mannose- binding protein carbohydrate-recognition domain trimerizes through a triple α-helical coiled-coil. Nat Struct. Biol. 1, 789-794.
    • (1994) Nat Struct. Biol. , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.B.3
  • 5
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis, W.I. & Drickamer, K. (1994). Trimeric structure of a C-type mannose-binding protein. Structure 2, 1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 6
    • 0027957760 scopus 로고
    • Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains
    • Graves, B.J., & Burns, D.K., et al., (1994). Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains. Nature 367, 532-538.
    • (1994) Nature , vol.367 , pp. 532-538
    • Graves, B.J.1    Burns, D.K.2
  • 7
    • 0032492659 scopus 로고    scopus 로고
    • The solution structure of type II antifreeze protein reveals a new member of the lectin family
    • Gronwald, W., & Sykes, B.D., et al., (1998). The solution structure of type II antifreeze protein reveals a new member of the lectin family. Biochemistry 37, 4712-4721.
    • (1998) Biochemistry , vol.37 , pp. 4712-4721
    • Gronwald, W.1    Sykes, B.D.2
  • 9
    • 0030744877 scopus 로고    scopus 로고
    • Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an α-helical coiled-coil
    • Nielsen, B.B., & Larsen, I.K., et al., (1997). Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an α-helical coiled-coil. FEBS Lett. 412, 388-396.
    • (1997) FEBS Lett. , vol.412 , pp. 388-396
    • Nielsen, B.B.1    Larsen, I.K.2
  • 10
    • 0028774709 scopus 로고
    • Trimeric C-type lectin domains in host defence
    • Hoppe, H.-J. & Reid, K.B.M. (1994). Trimeric C-type lectin domains in host defence. Structure 2, 1129-1133.
    • (1994) Structure , vol.2 , pp. 1129-1133
    • Hoppe, H.-J.1    Reid, K.B.M.2
  • 11
    • 0028233879 scopus 로고
    • Molecular structure of pulmonary surfactant protein D (SP-D)
    • Crouch, E., Persson, A., Chang, D. & Heuser, J. (1994). Molecular structure of pulmonary surfactant protein D (SP-D). J. Biol. Chem. 269, 17311-17319.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17311-17319
    • Crouch, E.1    Persson, A.2    Chang, D.3    Heuser, J.4
  • 12
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E.K., Klemm, J.D., Kim, P.S. & Alber, T. (1991 ). X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 13
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P.B., Kim, P.S. & Alber, T. (1994). Crystal structure of an isoleucine-zipper trimer. Nature 371, 80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 14
    • 0031023335 scopus 로고    scopus 로고
    • The crystal structure of the trimeric coiled coil coil-Vala: Implications for engineering crystals and supermolecular assemblies
    • Ogihara, N.L., Weiss, M.S., Degrado, W.F. & Eisenberg, D. (1997). The crystal structure of the trimeric coiled coil coil-Vala: Implications for engineering crystals and supermolecular assemblies. Protein Sci. 6, 80-88.
    • (1997) Protein Sci. , vol.6 , pp. 80-88
    • Ogihara, N.L.1    Weiss, M.S.2    Degrado, W.F.3    Eisenberg, D.4
  • 16
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coils
    • Crick, F.H.C. (1953). The packing of alpha-helices: Simple coiled- coils. Acta Crystallogr. 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 17
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S. & Alber, T. (1993). A switch between two-, three-, and four-stranded coiled coils in GCN4 zipper mutants. Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 18
    • 0030987407 scopus 로고    scopus 로고
    • A program for predicting two- or three-stranded coiled-coils
    • Wolf, E., Kim, P.S. & Berger, R. (1997). A program for predicting two- or three-stranded coiled-coils. Protein Sci. 6, 1179-1189.
    • (1997) Protein Sci. , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, R.3
  • 19
    • 0026696318 scopus 로고
    • Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli binding protein in bronchoalveolar lavage
    • Kuan, S.F., Rust, K. & Crouch, E. (1992). Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli binding protein in bronchoalveolar lavage. J. Clin. Invest. 90, 97-106.
    • (1992) J. Clin. Invest. , vol.90 , pp. 97-106
    • Kuan, S.F.1    Rust, K.2    Crouch, E.3
  • 21
    • 0030758115 scopus 로고    scopus 로고
    • Binding of pulmonary surfactant proteins A and D to Aspergillus fumigatus conidia enhances phagocytosis and killing by human neutrophils and alveolar macrophages
    • Madan, T., & Reid, K.B.M., et al., (1997). Binding of pulmonary surfactant proteins A and D to Aspergillus fumigatus conidia enhances phagocytosis and killing by human neutrophils and alveolar macrophages. Infect. Immun. 65, 3171-3179.
    • (1997) Infect. Immun. , vol.65 , pp. 3171-3179
    • Madan, T.1    Reid, K.B.M.2
  • 22
    • 0030807828 scopus 로고    scopus 로고
    • Lung surfactant proteins A and D can inhibit specific ige binding to the allergens of Aspergillus fumigatus and block allergen-induced histamine release from human basophils
    • Madan, T., & Reid, K.B.M., et al., (1997). Lung surfactant proteins A and D can inhibit specific ige binding to the allergens of Aspergillus fumigatus and block allergen-induced histamine release from human basophils. Clin. Exp. Immunol. 110, 241-249.
    • (1997) Clin. Exp. Immunol. , vol.110 , pp. 241-249
    • Madan, T.1    Reid, K.B.M.2
  • 23
    • 0031799387 scopus 로고    scopus 로고
    • Pulmonary surfactant proteins A and D enhance neutrophil uptake of bacteria
    • Hartshorn, K.L., & Sastry, K.N., et al., (1998). Pulmonary surfactant proteins A and D enhance neutrophil uptake of bacteria. Am. J. Physiol. 247, L958-L969.
    • (1998) Am. J. Physiol. , vol.247
    • Hartshorn, K.L.1    Sastry, K.N.2
  • 24
    • 0027532105 scopus 로고
    • Pitch diversity in α-helical coiled coils
    • Seo, J. & Cohen, C. (1993). Pitch diversity in α-helical coiled coils. Proteins 15, 223-234.
    • (1993) Proteins , vol.15 , pp. 223-234
    • Seo, J.1    Cohen, C.2
  • 25
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis, W.I., Drickamer, K. & Hendrickson, W.A. (1992). Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 26
    • 0030069340 scopus 로고    scopus 로고
    • Structural analysis of monosaccharide recognition by rat liver mannose-binding protein
    • Ng, K.-S., Drickamer, K. & Weis, W.I. (1996). Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. J. Biol. Chem. 271, 663-674.
    • (1996) J. Biol. Chem. , vol.271 , pp. 663-674
    • Ng, K.-S.1    Drickamer, K.2    Weis, W.I.3
  • 27
    • 0242405758 scopus 로고    scopus 로고
    • Distribution of solvent and ligand molecules around aromatic sidechains and its implication on carbonic anhydrase catalytic mechanism
    • Håkansson, K. (1996). Distribution of solvent and ligand molecules around aromatic sidechains and its implication on carbonic anhydrase catalytic mechanism. Int. J. Biol. Macromol. 18, 189-194.
    • (1996) Int. J. Biol. Macromol. , vol.18 , pp. 189-194
    • Håkansson, K.1
  • 28
    • 0029974730 scopus 로고    scopus 로고
    • An engineered allosteric switch in leucine-zipper oligomerization
    • Gonzalez, L. Jr., Plecs, J.J. & Alber, T. (1996). An engineered allosteric switch in leucine-zipper oligomerization. Nat. Struct. Biol. 3, 510-515.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 510-515
    • Gonzalez L., Jr.1    Plecs, J.J.2    Alber, T.3
  • 29
    • 0028175514 scopus 로고
    • A parallel three stranded α-helical bundle at the nucleation site of collagen triple-helix formation
    • Hoppe, H.-J., Barlow, P.N. & Reid, K.B.M. (1994). A parallel three stranded α-helical bundle at the nucleation site of collagen triple-helix formation. FEBS Lett. 344, 191-195.
    • (1994) FEBS Lett. , vol.344 , pp. 191-195
    • Hoppe, H.-J.1    Barlow, P.N.2    Reid, K.B.M.3
  • 30
    • 0030925434 scopus 로고    scopus 로고
    • Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule
    • Holmskov, U., & Reid, K.B.M., et al., (1997). Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule. J. Biol. Chem. 272, 13743-13749.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13743-13749
    • Holmskov, U.1    Reid, K.B.M.2
  • 31
    • 0003976860 scopus 로고
    • SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). In Data Collection and Processing. pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 32
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMORE: An automated package for molecular replacement. Acta Crystallogr. A 50 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 33
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, K. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, K.2    Karplus, M.3
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Macarthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., & Tasumi, M., et al., (1977). The Protein Data Bank: A computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 40
    • 84986486656 scopus 로고
    • A rapid finite-difference algoritim, utilising successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A. & Honig, B.J. (1991). A rapid finite-difference algoritim, utilising successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem. 12, 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.