메뉴 건너뛰기




Volumn 39, Issue 5, 1999, Pages 969-978

Homology modelling of the core domain of the endogenous lectin comitin: Structural basis for its mannose-binding specificity

Author keywords

Comitin; Dictyostelium discoideum; Mannose binding specificity; Molecular modelling

Indexed keywords

COMITIN; CYTOSKELETON; DICTYOSTELIUM DISCOIDEUM; LECTIN; MANNOSE;

EID: 0033103881     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006133527621     Document Type: Article
Times cited : (8)

References (40)
  • 1
    • 0025050666 scopus 로고
    • Nucleotide sequence and expression of a cDNa encoding chick brain actin depolymerizing factor
    • Adams ME, Minamide LS, Duester G, Bamburg JR: Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor. Biochemistry 29: 7414-7420 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7414-7420
    • Adams, M.E.1    Minamide, L.S.2    Duester, G.3    Bamburg, J.R.4
  • 2
    • 0030727857 scopus 로고    scopus 로고
    • Glycogenin, the primer of glycogen synthesis, binds to actin
    • Baqué S, Guinovart JJ, Ferrer JC: Glycogenin, the primer of glycogen synthesis, binds to actin. FEBS Lett 417: 355-359 (1997).
    • (1997) FEBS Lett , vol.417 , pp. 355-359
    • Baqué, S.1    Guinovart, J.J.2    Ferrer, J.C.3
  • 3
    • 0030452169 scopus 로고    scopus 로고
    • Structure-function relationship of monocot mannose-binding lectins
    • Barre A, Van Damme EJM, Peumans WJ, Rougé P: Structure-function relationship of monocot mannose-binding lectins. Plant Physiol 112: 1531-1540 (1996).
    • (1996) Plant Physiol , vol.112 , pp. 1531-1540
    • Barre, A.1    Van Damme, E.J.M.2    Peumans, W.J.3    Rougé, P.4
  • 5
    • 0030812616 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic studies on the mannose-specific lectin from garlic
    • Chandra NR, Dam T, Surolia A, Vijayan M: Crystallization and preliminary crystallographic studies on the mannose-specific lectin from garlic. Acta Crystallogr Sect D 53: 787-788 (1997).
    • (1997) Acta Crystallogr Sect D , vol.53 , pp. 787-788
    • Chandra, N.R.1    Dam, T.2    Surolia, A.3    Vijayan, M.4
  • 6
    • 0030499408 scopus 로고    scopus 로고
    • X-ray structure solution of Amaryllis lectin by molecular replacement with only 4% of the total diffracting matter
    • Chantalat L, Wood SD, Rizkallah PJ, Reynolds CD: X-ray structure solution of Amaryllis lectin by molecular replacement with only 4% of the total diffracting matter. Acta Crystallogr Sect D 52: 1146-1152 (1996).
    • (1996) Acta Crystallogr Sect D , vol.52 , pp. 1146-1152
    • Chantalat, L.1    Wood, S.D.2    Rizkallah, P.J.3    Reynolds, C.D.4
  • 7
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4: Acta Crystallogry Sect D 50: 760-763 (1994).
    • (1994) Acta Crystallogry Sect D , vol.50 , pp. 760-763
  • 8
    • 0023657949 scopus 로고
    • Hydrophobie cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP: Hydrophobie cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 224: 149-155 (1987).
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 9
    • 0023280069 scopus 로고
    • Calculation of electrostatic potential in an enzyme active site
    • Gilson MK, Honing BH: Calculation of electrostatic potential in an enzyme active site. Nature 330: 84-86 (1987).
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honing, B.H.2
  • 10
    • 0022820961 scopus 로고
    • Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNa splicing and polyadenylation
    • Helfman DM, Cheley S, Kuismanen E, Finn LA, Yamawaki-Kataota Y: Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation. Mol Cell Biol 6: 3582-3595 (1986).
    • (1986) Mol Cell Biol , vol.6 , pp. 3582-3595
    • Helfman, D.M.1    Cheley, S.2    Kuismanen, E.3    Finn, L.A.4    Yamawaki-Kataota, Y.5
  • 11
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester G, Kaku H, Goldstein U, Wright CS: Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nature Struct Biol 2: 472-479 (1995).
    • (1995) Nature Struct Biol , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, U.3    Wright, C.S.4
  • 12
    • 0030568976 scopus 로고    scopus 로고
    • The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- And dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 Å and 3.0 Å resolution
    • Hester G, Wright CS: The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 Å and 3.0 Å resolution. J Mol Biol 262: 516-531 (1996).
    • (1996) J Mol Biol , vol.262 , pp. 516-531
    • Hester, G.1    Wright, C.S.2
  • 13
    • 0024246956 scopus 로고
    • Surface, subunit interface and interior of oligomeric proteins
    • Janin J, Miller S, Chothia C: Surface, subunit interface and interior of oligomeric proteins. J Mol Biol 204: 155-164 (1988).
    • (1988) J Mol Biol , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 14
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton J: Principles of protein-protein interactions. Proc Natl Acad Sci USA 93: 13-20 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.2
  • 15
    • 0028347643 scopus 로고
    • The actin binding site in the tail domain of Dictyostelium mysosin IC (myoC) within the glycine- And proline-rich sequence (tail homology region 2)
    • Jung G, Hammer JA: The actin binding site in the tail domain of Dictyostelium mysosin IC (myoC) within the glycine- and proline-rich sequence (tail homology region 2). FEBS Lett 342: 197-202 (1994).
    • (1994) FEBS Lett , vol.342 , pp. 197-202
    • Jung, G.1    Hammer, J.A.2
  • 16
    • 0029958869 scopus 로고    scopus 로고
    • Linking microfilaments to intracellular membranes: The actin-binding and vesicle-associated protein comitin exhibits a mannose-specific lectin activity
    • Jung E, Fucini P, Stewart M, Noegel AA, Schleicher M: Linking microfilaments to intracellular membranes: the actin-binding and vesicle-associated protein comitin exhibits a mannose-specific lectin activity. EMBO J 15: 1238-1246 (1996).
    • (1996) EMBO J , vol.15 , pp. 1238-1246
    • Jung, E.1    Fucini, P.2    Stewart, M.3    Noegel, A.A.4    Schleicher, M.5
  • 18
    • 0026170577 scopus 로고
    • Interaction of five D-mannose specific lectins with a series of synthetic branched trisaccharides
    • Kaku H, Goldstein U, Oscarson S: Interaction of five D-mannose specific lectins with a series of synthetic branched trisaccharides. Carbohydrate Res 213: 109-116 (1991).
    • (1991) Carbohydrate Res , vol.213 , pp. 109-116
    • Kaku, H.1    Goldstein, U.2    Oscarson, S.3
  • 19
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ: Molscript: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24: 946-950 (1991).
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedure to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot, L, Henrissat B, Gaboriaud C, Bissery V, Morgat A, Mornon JP: Hydrophobic cluster analysis: procedure to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72: 555-574 (1990).
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 23
    • 0028225890 scopus 로고
    • Structure of baby hamster kidney carbohydrate-binding protein CBP30, and S-type animal lectin
    • Mehul B, Bawumia S, Martin SR, Hughes RC: Structure of baby hamster kidney carbohydrate-binding protein CBP30, and S-type animal lectin. J Biol Chem 269: 18250-18258 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 18250-18258
    • Mehul, B.1    Bawumia, S.2    Martin, S.R.3    Hughes, R.C.4
  • 25
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • Miller S, Lesk AM, Janin J, Chothia C: The accessible surface area and stability of oligomeric proteins. Nature 328: 843-836 (1987).
    • (1987) Nature , vol.328 , pp. 843-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 27
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B: Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 28
    • 0025293774 scopus 로고
    • A protein with homology to the C-terminal repeat of octopus rhodopsin and synaptophysin is a member of a multigene family in Dictyostelium discoideum
    • Noegel AA, Gerisch G, Lottspeich F, Schleicher M: A protein with homology to the C-terminal repeat of octopus rhodopsin and synaptophysin is a member of a multigene family in Dictyostelium discoideum. FEBS Lett 266: 118-122 (1990).
    • (1990) FEBS Lett , vol.266 , pp. 118-122
    • Noegel, A.A.1    Gerisch, G.2    Lottspeich, F.3    Schleicher, M.4
  • 31
    • 0028231727 scopus 로고
    • The GPQ-rich segment of Dictyostelium myosin IB contains an actin binding site
    • Rosenfeld SS, Rener B: The GPQ-rich segment of Dictyostelium myosin IB contains an actin binding site. Biochemistry 33: 2322-2328 (1994).
    • (1994) Biochemistry , vol.33 , pp. 2322-2328
    • Rosenfeld, S.S.1    Rener, B.2
  • 32
    • 0021928968 scopus 로고
    • Isolation of an actin binding protein from membranes of Dictyostelium discoideum
    • Stratford CA, Brown SS: Isolation of an actin binding protein from membranes of Dictyostelium discoideum. J Cell Biol 100: 727-735 (1985).
    • (1985) J Cell Biol , vol.100 , pp. 727-735
    • Stratford, C.A.1    Brown, S.S.2
  • 33
    • 0001035146 scopus 로고
    • Isolation and characterization of a lectin with exclusive specificity toward mannose from snowdrop (Galanthus nivalis) bulbs
    • Van Damme EJM, Allen AK, Peumans WJ: Isolation and characterization of a lectin with exclusive specificity toward mannose from snowdrop (Galanthus nivalis) bulbs. FEBS Lett 215: 140-144 (1987).
    • (1987) FEBS Lett , vol.215 , pp. 140-144
    • Van Damme, E.J.M.1    Allen, A.K.2    Peumans, W.J.3
  • 35
    • 0028004248 scopus 로고
    • The GPI anchor of cell-surface proteins is synthesized on the cytoplasmic face of the endoplasmic reticulum
    • Vidugiriene J, Menon AK: The GPI anchor of cell-surface proteins is synthesized on the cytoplasmic face of the endoplasmic reticulum. J Cell Biol 127: 333-341 (1994).
    • (1994) J Cell Biol , vol.127 , pp. 333-341
    • Vidugiriene, J.1    Menon, A.K.2
  • 36
    • 0027361181 scopus 로고
    • The actin-binding protein comitin (p24) is a component of the Golgi apparatus
    • Weiner OH, Murphy J, Griffiths G, Schleicher M, Noegel AA: The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J Cell Biol 123: 23-34 (1993).
    • (1993) J Cell Biol , vol.123 , pp. 23-34
    • Weiner, O.H.1    Murphy, J.2    Griffiths, G.3    Schleicher, M.4    Noegel, A.A.5
  • 37
    • 0032500567 scopus 로고    scopus 로고
    • Cofilin and gelsolin segment-1: Molecular dynamics simulation and biochemical analysis predict a similar actin binding mode
    • Wriggers W, Tang JX, Azuma T, Marks PW, Janmey PA: Cofilin and gelsolin segment-1: molecular dynamics simulation and biochemical analysis predict a similar actin binding mode. J Mol Biol 282: 921-932 (1998).
    • (1998) J Mol Biol , vol.282 , pp. 921-932
    • Wriggers, W.1    Tang, J.X.2    Azuma, T.3    Marks, P.W.4    Janmey, P.A.5
  • 38
    • 0029658497 scopus 로고    scopus 로고
    • The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: Evidence for two unique binding modes
    • Wright CS, Hester G: The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes. Structure 11: 1339-1352 (1996).
    • (1996) Structure , vol.11 , pp. 1339-1352
    • Wright, C.S.1    Hester, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.