메뉴 건너뛰기




Volumn 32, Issue 11, 2002, Pages 1577-1583

A structural model of the chitin-binding domain of cuticle proteins

Author keywords

Antiparallel pleated sheet half barrel; Chitin; Cuticle proteins; Homology modelling; Protein carbohydrate interactions; Retinol binding protein; Structural model

Indexed keywords

AROMATIC COMPOUND; CHITIN; PLASMA PROTEIN; POLYSACCHARIDE; PROTEIN; RETINOL BINDING PROTEIN; CUTICLE PROTEINS, INSECTS; INSECT PROTEIN;

EID: 0036837102     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(02)00079-6     Document Type: Article
Times cited : (84)

References (38)
  • 3
    • 51249171625 scopus 로고
    • Conformations in polysaccharides and complex carbohydrates. Proceedings of the International Symposium on Biomolecular Structure Interactions
    • Atkins, E.D.T., 1985. Conformations in polysaccharides and complex carbohydrates. Proceedings of the International Symposium on Biomolecular Structure Interactions, Suppl. J. Biosci. 8, Nos 1-2, 375-387.
    • (1985) Suppl. J. Biosci. , vol.8 , Issue.1-2 , pp. 375-387
    • Atkins, E.D.T.1
  • 5
    • 0028674953 scopus 로고
    • Identification of the cDNA, gene and promoter for a major protein from flexible cuticles of the giant silkmoth Hyalophora cecropia
    • Binger, L.C., Willis, J.H., 1994. Identification of the cDNA, gene and promoter for a major protein from flexible cuticles of the giant silkmoth Hyalophora cecropia. Insect Biochem. Molec. Biol. 24, 989-1000.
    • (1994) Insect Biochem. Molec. Biol. , vol.24 , pp. 989-1000
    • Binger, L.C.1    Willis, J.H.2
  • 6
    • 0019324851 scopus 로고
    • Structure of chitin-protein complexes: Ovipositor of the ichneumon fly Megarhyssa
    • Blackwell, J., Weih, M.A., 1980. Structure of chitin-protein complexes: ovipositor of the ichneumon fly Megarhyssa. J. Mol. Biol. 137, 49-60.
    • (1980) J. Mol. Biol. , vol.137 , pp. 49-60
    • Blackwell, J.1    Weih, M.A.2
  • 7
    • 0034968405 scopus 로고    scopus 로고
    • Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TÜ901
    • Campos-Olivas, R., Hörr, I., Bormann, C., Jung, G., Gronenbom, A.M., 2001. Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TÜ901. J. Mol. Biol. 308, 765-782.
    • (2001) J. Mol. Biol. , vol.308 , pp. 765-782
    • Campos-Olivas, R.1    Hörr, I.2    Bormann, C.3    Jung, G.4    Gronenbom, A.M.5
  • 11
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: Structural and sequence overview
    • Flower, D.R., North, A.C.T., Sansom, C.E., 2000. The lipocalin protein family: structural and sequence overview. Biochim. Biophys. Acta 1482, 9-24.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.T.2    Sansom, C.E.3
  • 12
    • 0000112938 scopus 로고
    • The structure of insect cuticles
    • Fraenkel, G., Rudall, K.M., 1947. The structure of insect cuticles. Proc. Roy. Soc. B 34, 111-143.
    • (1947) Proc. Roy. Soc. B , vol.34 , pp. 111-143
    • Fraenkel, G.1    Rudall, K.M.2
  • 13
    • 0000463917 scopus 로고
    • Some conformational studies of larval cuticular proteins from Calliphora vicina
    • Hackman, R.H., Goldberg, M., 1979. Some conformational studies of larval cuticular proteins from Calliphora vicina. Insect Biochem 9, 557-561.
    • (1979) Insect Biochem. , vol.9 , pp. 557-561
    • Hackman, R.H.1    Goldberg, M.2
  • 14
    • 0024110035 scopus 로고
    • A protein secondary structure prediction scheme for the IBM PC and compatibles
    • Hamodrakas, S.J., 1988. A protein secondary structure prediction scheme for the IBM PC and compatibles. CABIOS 4, 473-477.
    • (1988) CABIOS , vol.4 , pp. 473-477
    • Hamodrakas, S.J.1
  • 15
    • 0027017218 scopus 로고
    • Molecular architecture of helicoidal proteinaceous eggshells
    • Case, S.T. (Ed.), Springer-Verlag, Berlin, Heidelberg
    • Hamodrakas, S.J., 1992. Molecular architecture of helicoidal proteinaceous eggshells. In: Case, S.T. (Ed.), Results and Problems in Cell Differentiation, vol. 19. Springer-Verlag, Berlin, Heidelberg, pp. 116-186.
    • (1992) Results and Problems in Cell Differentiation , vol.19 , pp. 116-186
    • Hamodrakas, S.J.1
  • 16
    • 0030699965 scopus 로고    scopus 로고
    • The crystal structure of the complex of Concanavalin A with 4′methylumbelliferyl-α-D-glucopyranoside
    • Hamodrakas, S.J., Kanellopoulos, P.N., Pavlou, K., Tucker, P.A., 1997. The crystal structure of the complex of Concanavalin A with 4′methylumbelliferyl-α-D-glucopyranoside. J. Struct. Biol. 118, 23-30.
    • (1997) J. Struct. Biol. , vol.118 , pp. 23-30
    • Hamodrakas, S.J.1    Kanellopoulos, P.N.2    Pavlou, K.3    Tucker, P.A.4
  • 17
    • 0033103766 scopus 로고    scopus 로고
    • Is β-pleated sheet the molecular conformation which dictates the formation of the helicoidal cuticle?
    • Iconomidou, V.A., Willis, J.H., Hamodrakas, S.J., 1999. Is β-pleated sheet the molecular conformation which dictates the formation of the helicoidal cuticle? Insect Biochem. Mol. Biol. 29, 285-292.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 285-292
    • Iconomidou, V.A.1    Willis, J.H.2    Hamodrakas, S.J.3
  • 19
    • 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. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 22
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., Honig, B., 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 23
    • 0030631524 scopus 로고    scopus 로고
    • Evolution of immunoglobulin-like modules in chitinases: Their structural flexibility and functional implications
    • Perrakis, A., Ouzounis, C., Wilson, K.S., 1997. Evolution of immunoglobulin-like modules in chitinases: their structural flexibility and functional implications. Folding and Design 2, 291-294.
    • (1997) Folding and Design , vol.2 , pp. 291-294
    • Perrakis, A.1    Ouzounis, C.2    Wilson, K.S.3
  • 24
    • 0023688992 scopus 로고
    • Structure and expression of a Manduca sexta larval cuticle gene homologous to Drosophila cuticle genes
    • Rebers, J.E., Riddiford, L.M., 1988. Structure and expression of a Manduca sexta larval cuticle gene homologous to Drosophila cuticle genes. J. Mol. Biol. 203, 411-423.
    • (1988) J. Mol. Biol. , vol.203 , pp. 411-423
    • Rebers, J.E.1    Riddiford, L.M.2
  • 25
    • 0034804735 scopus 로고    scopus 로고
    • A conserved domain in arthropod cuticular proteins binds chitin
    • Rebers, J.F., Willis, J.H., 2001. A conserved domain in arthropod cuticular proteins binds chitin. Insect Biochem Mol. Biol. 31, 1083-1093.
    • (2001) Insect Biochem Mol. Biol. , vol.31 , pp. 1083-1093
    • Rebers, J.F.1    Willis, J.H.2
  • 27
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost, B., 1996. PHD: Predicting one-dimensional protein structure by profile based neural networks. Meth. In Enzym. 266, 525-539.
    • (1996) Meth. In Enzym. , vol.266 , pp. 525-539
    • Rost, B.1
  • 28
    • 0034674709 scopus 로고    scopus 로고
    • Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif
    • Suetake, T., Tsuda, S., Kawabata, S., Miura, K., Iwanaga, S., Hikichi, K., Nitta, K., Kawano, K., 2000. Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. J. Biol. Chem. 275 (24), 17929-17932.
    • (2000) J. Biol. Chem. , vol.275 , Issue.24 , pp. 17929-17932
    • Suetake, T.1    Tsuda, S.2    Kawabata, S.3    Miura, K.4    Iwanaga, S.5    Hikichi, K.6    Nitta, K.7    Kawano, K.8
  • 29
  • 30
    • 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., Higgins, D.G., Gibson, T.J., 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
  • 31
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo, J., Lamed, R., Chirino, A.J., Morag, E., Bayer, E.A., Shoham, Y., Steitz, T.A., 1996. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 15, 5739-5751.
    • (1996) EMBO J. , vol.15 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 32
    • 0035798612 scopus 로고    scopus 로고
    • Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170
    • Uchiyama, T., Katouno, F., Nikaidou, N., Nonaka, T., Sugiyama, J., Watanabe, T., 2001. Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170. J. Biol. Chem. 276 (44), 41343-41349.
    • (2001) J. Biol. Chem. , vol.276 , Issue.44 , pp. 41343-41349
    • Uchiyama, T.1    Katouno, F.2    Nikaidou, N.3    Nonaka, T.4    Sugiyama, J.5    Watanabe, T.6
  • 34
    • 0030248996 scopus 로고    scopus 로고
    • Low-resolution docking: Prediction of complexes for undetermined structures
    • Vakser, I.A., 1996. Low-resolution docking: Prediction of complexes for undetermined structures. Biopolymers 39, 455-464.
    • (1996) Biopolymers , vol.39 , pp. 455-464
    • Vakser, I.A.1
  • 35
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design package
    • Vriend, G., 1990. WHAT IF: A molecular modeling and drug design package. J. Mol. Graph. 8, 52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 36
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas, N.K., 1991. Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol. 1, 732-740.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 37
    • 22644452601 scopus 로고    scopus 로고
    • Cuticular proteins in insects and crustaceans
    • Willis, J.H., 1999. Cuticular proteins in insects and crustaceans. Am. Zool 39, 600-609.
    • (1999) Am. Zool , vol.39 , pp. 600-609
    • Willis, J.H.1
  • 38
    • 0027960222 scopus 로고
    • Crystallographic studies on complexes between retinoids and plasma retinol-binding protein
    • Zanotti, G., Marcello, M., Malpeli, G., Folli, C., Sartori, G., Berni, R., 1994. Crystallographic studies on complexes between retinoids and plasma retinol-binding protein. J. Biol. Chem. 269, 29613-29620.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29613-29620
    • Zanotti, G.1    Marcello, M.2    Malpeli, G.3    Folli, C.4    Sartori, G.5    Berni, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.