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Volumn 11, Issue 10, 2003, Pages 1291-1301

Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN; NERVE CELL ADHESION MOLECULE;

EID: 2342508857     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.09.006     Document Type: Article
Times cited : (150)

References (52)
  • 2
    • 0035800660 scopus 로고    scopus 로고
    • Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: Can solution studies define the mechanism of homophilic binding?
    • Atkins A.R., Chung J., Deechongkit S., Little E.B., Edelman G.M., Wright P.E., Cunningham B.A., Dyson H.J. Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM. can solution studies define the mechanism of homophilic binding? J. Mol. Biol. 311:2001;161-172.
    • (2001) J. Mol. Biol. , vol.311 , pp. 161-172
    • Atkins, A.R.1    Chung, J.2    Deechongkit, S.3    Little, E.B.4    Edelman, G.M.5    Wright, P.E.6    Cunningham, B.A.7    Dyson, H.J.8
  • 5
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork P., Downing A.K., Kieffer B., Campbell I.D. Structure and distribution of modules in extracellular proteins. Q. Rev. Biophys. 29:1996;119-167.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 6
    • 0029998613 scopus 로고    scopus 로고
    • Lateral dimerization is required for the homophilic binding activity of C-cadherin
    • Brieher W.M., Yap A.S., Gumbiner B.M. Lateral dimerization is required for the homophilic binding activity of C-cadherin. J. Cell Biol. 135:1996;487-496.
    • (1996) J. Cell Biol. , vol.135 , pp. 487-496
    • Brieher, W.M.1    Yap, A.S.2    Gumbiner, B.M.3
  • 8
    • 0032516060 scopus 로고    scopus 로고
    • A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1
    • Casasnovas J.M., Stehle T., Liu J.H., Wang J.H., Springer T.A. A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1. Proc. Natl. Acad. Sci. USA. 95:1998;4134-4139.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4134-4139
    • Casasnovas, J.M.1    Stehle, T.2    Liu, J.H.3    Wang, J.H.4    Springer, T.A.5
  • 9
    • 0030907070 scopus 로고    scopus 로고
    • The molecular structure of cell adhesion molecules
    • Chothia C., Jones E.Y. The molecular structure of cell adhesion molecules. Annu. Rev. Biochem. 66:1997;823-862.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 823-862
    • Chothia, C.1    Jones, E.Y.2
  • 10
    • 0024610031 scopus 로고
    • Identification of a heparin binding domain of the neural cell adhesion molecule N-CAM using synthetic peptides
    • Cole G.J., Akeson R. Identification of a heparin binding domain of the neural cell adhesion molecule N-CAM using synthetic peptides. Neuron. 2:1989;1157-1165.
    • (1989) Neuron , vol.2 , pp. 1157-1165
    • Cole, G.J.1    Akeson, R.2
  • 11
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4) The CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 12
    • 0345095249 scopus 로고
    • Neural cell adhesion molecule (NCAM) accumulates in denervated and paralyzed skeletal muscles
    • Covault J., Sanes J.R. Neural cell adhesion molecule (NCAM) accumulates in denervated and paralyzed skeletal muscles. Proc. Natl. Acad. Sci. USA. 82:1985;4544-4548.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4544-4548
    • Covault, J.1    Sanes, J.R.2
  • 13
    • 0023186308 scopus 로고
    • Neural cell adhesion molecule: Structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing
    • Cunningham B.A., Hemperly J.J., Murray B.A., Prediger E.A., Brackenbury R., Edelman G.M. Neural cell adhesion molecule. structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing Science. 236:1987;799-806.
    • (1987) Science , vol.236 , pp. 799-806
    • Cunningham, B.A.1    Hemperly, J.J.2    Murray, B.A.3    Prediger, E.A.4    Brackenbury, R.5    Edelman, G.M.6
  • 14
    • 0028153795 scopus 로고
    • Planar stacking interactions of arginine and aromatic side-chains in proteins
    • Flocco M.M., Mowbray S.L. Planar stacking interactions of arginine and aromatic side-chains in proteins. J. Mol. Biol. 235:1994;709-717.
    • (1994) J. Mol. Biol. , vol.235 , pp. 709-717
    • Flocco, M.M.1    Mowbray, S.L.2
  • 15
    • 0034640117 scopus 로고    scopus 로고
    • The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion
    • Freigang J., Proba K., Leder L., Diederichs K., Sonderegger P., Welte W. The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion. Cell. 101:2000;425-433.
    • (2000) Cell , vol.101 , pp. 425-433
    • Freigang, J.1    Proba, K.2    Leder, L.3    Diederichs, K.4    Sonderegger, P.5    Welte, W.6
  • 16
    • 0000046089 scopus 로고
    • A human beta-actin expression vector system directs high-level accumulation of antisense transcripts
    • Gunning P., Leavitt J., Muscat G., Ng S.Y., Kedes L. A human beta-actin expression vector system directs high-level accumulation of antisense transcripts. Proc. Natl. Acad. Sci. USA. 84:1987;4831-4835.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4831-4835
    • Gunning, P.1    Leavitt, J.2    Muscat, G.3    Ng, S.Y.4    Kedes, L.5
  • 17
    • 0023192060 scopus 로고
    • Visualization of neural cell adhesion molecule by electron microscopy
    • Hall A.K., Rutishauser U. Visualization of neural cell adhesion molecule by electron microscopy. J. Cell Biol. 104:1987;1579-1586.
    • (1987) J. Cell Biol. , vol.104 , pp. 1579-1586
    • Hall, A.K.1    Rutishauser, U.2
  • 18
    • 0030456773 scopus 로고    scopus 로고
    • Evidence for regulated dimerization of cell-cell adhesion molecule (C-CAM) in epithelial cells
    • Hunter I., Sawa H., Edlund M., Öbrink B. Evidence for regulated dimerization of cell-cell adhesion molecule (C-CAM) in epithelial cells. Biochem. J. 320:1996;847-853.
    • (1996) Biochem. J. , vol.320 , pp. 847-853
    • Hunter, I.1    Sawa, H.2    Edlund, M.3    Öbrink, B.4
  • 19
    • 0031297461 scopus 로고    scopus 로고
    • Specific versus non-specific contacts in protein crystals
    • Janin J. Specific versus non-specific contacts in protein crystals. Nat. Struct. Biol. 4:1997;973-974.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 973-974
    • Janin, J.1
  • 22
    • 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;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
  • 23
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2
    • Jones E.Y., Davis S.J., Williams A.F., Harlos K., Stuart D.I. Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Nature. 360:1992;232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 24
    • 0026448194 scopus 로고
    • The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans
    • Kallapur S.G., Akeson R.A. The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans. J. Neurosci. Res. 33:1992;538-548.
    • (1992) J. Neurosci. Res. , vol.33 , pp. 538-548
    • Kallapur, S.G.1    Akeson, R.A.2
  • 25
    • 0029911373 scopus 로고    scopus 로고
    • Functional characterization of NCAM fibronectin type III domains: Demonstration of modulatory effects of the proline-rich sequence encoded by alternatively spliced exons a and AAG
    • Kasper C., Stahlhut M., Berezin V., Maar T.E., Edvardsen K., Kiselyov V.V., Soroka V., Bock E. Functional characterization of NCAM fibronectin type III domains. demonstration of modulatory effects of the proline-rich sequence encoded by alternatively spliced exons a and AAG J. Neurosci. Res. 46:1996;173-186.
    • (1996) J. Neurosci. Res. , vol.46 , pp. 173-186
    • Kasper, C.1    Stahlhut, M.2    Berezin, V.3    Maar, T.E.4    Edvardsen, K.5    Kiselyov, V.V.6    Soroka, V.7    Bock, E.8
  • 27
    • 0030899695 scopus 로고    scopus 로고
    • The first Ig-like NCAM domain is involved in both double reciprocal interaction with the second Ig-like NCAM domain and in heparin binding
    • Kiselyov V.V., Berezin V., Maar T., Soroka V., Edvardsen K., Schousboe A., Bock E. The first Ig-like NCAM domain is involved in both double reciprocal interaction with the second Ig-like NCAM domain and in heparin binding. J. Biol. Chem. 272:1997;10125-10134.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10125-10134
    • Kiselyov, V.V.1    Berezin, V.2    Maar, T.3    Soroka, V.4    Edvardsen, K.5    Schousboe, A.6    Bock, E.7
  • 28
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt G.J., Jones T.A. Phi/psi-chology. Ramachandran revisited Structure. 4:1996;1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 29
    • 0034653487 scopus 로고    scopus 로고
    • Neural cell adhesion molecule-stimulated neurite outgrowth depends on activation of protein kinase C and the Ras-mitogen-activated protein kinase pathway
    • Kolkova K., Novitskaya V., Pedersen N., Berezin V., Bock E. Neural cell adhesion molecule-stimulated neurite outgrowth depends on activation of protein kinase C and the Ras-mitogen-activated protein kinase pathway. J. Neurosci. 20:2000;2238-2246.
    • (2000) J. Neurosci. , vol.20 , pp. 2238-2246
    • Kolkova, K.1    Novitskaya, V.2    Pedersen, N.3    Berezin, V.4    Bock, E.5
  • 31
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy D.J., Aukhil I., Erickson H.P. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell. 84:1996;155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 33
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 34
    • 12444275335 scopus 로고
    • Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules
    • Milev P., Friedlander D.R., Sakurai T., Karthikeyan L., Flad M., Margolis R.K., Grummet M., Margolis R.U. Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules. J. Cell Biol. 121:1994;1409-1421.
    • (1994) J. Cell Biol. , vol.121 , pp. 1409-1421
    • Milev, P.1    Friedlander, D.R.2    Sakurai, T.3    Karthikeyan, L.4    Flad, M.5    Margolis, R.K.6    Grummet, M.7    Margolis, R.U.8
  • 35
    • 0034614555 scopus 로고    scopus 로고
    • Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interactions
    • Miyahara M., Nakanishi H., Takahashi K., Satoh-Horikawa K., Tachibana K., Takai Y. Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interactions. J. Biol. Chem. 275:2000;613-618.
    • (2000) J. Biol. Chem. , vol.275 , pp. 613-618
    • Miyahara, M.1    Nakanishi, H.2    Takahashi, K.3    Satoh-Horikawa, K.4    Tachibana, K.5    Takai, Y.6
  • 36
    • 0031053055 scopus 로고    scopus 로고
    • AmoRe: An automated molecular replacement program package
    • Navaza J., Saludjian P. AmoRe. an automated molecular replacement program package Methods Enzymol. 276:1997;581-594.
    • (1997) Methods Enzymol. , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 37
    • 0024395344 scopus 로고
    • Equilibrium binding analysis of neural cell adhesion molecule binding to heparin
    • Nybroe O., Moran N., Bock E. Equilibrium binding analysis of neural cell adhesion molecule binding to heparin. J. Neurochem. 52:1989;1947-1949.
    • (1989) J. Neurochem. , vol.52 , pp. 1947-1949
    • Nybroe, O.1    Moran, N.2    Bock, E.3
  • 38
    • 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. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:1999;458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 40
    • 0024425966 scopus 로고
    • Binding properties of the neural cell adhesion molecule to different components of the extracellular matrix
    • Probstmeier R., Kuhn K., Schachner M. Binding properties of the neural cell adhesion molecule to different components of the extracellular matrix. J. Neurochem. 53:1989;1794-1801.
    • (1989) J. Neurochem. , vol.53 , pp. 1794-1801
    • Probstmeier, R.1    Kuhn, K.2    Schachner, M.3
  • 41
    • 0029867737 scopus 로고    scopus 로고
    • Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immunoglobulin domains
    • Ranheim T.S., Edelman G.M., Cunningham B.A. Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immunoglobulin domains. Proc. Natl. Acad. Sci. USA. 93:1996;4071-4075.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4071-4075
    • Ranheim, T.S.1    Edelman, G.M.2    Cunningham, B.A.3
  • 42
    • 0026670583 scopus 로고
    • Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM
    • Rao Y., Wu X.-F., Gariepy J., Rutishauser U., Siu C.-H. Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM. J. Cell Biol. 118:1992;937-949.
    • (1992) J. Cell Biol. , vol.118 , pp. 937-949
    • Rao, Y.1    Wu, X.-F.2    Gariepy, J.3    Rutishauser, U.4    Siu, C.-H.5
  • 43
    • 0028036803 scopus 로고
    • Mechanisms of homophilic binding mediated by the neural cell adhesion molecule NCAM. Evidence for isologous interaction
    • Rao Y., Zhao X., Siu C.-H. Mechanisms of homophilic binding mediated by the neural cell adhesion molecule NCAM. Evidence for isologous interaction. J. Biol. Chem. 269:1994;27540-27548.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27540-27548
    • Rao, Y.1    Zhao, X.2    Siu, C.-H.3
  • 45
    • 0028236467 scopus 로고
    • The homophilic binding site of the neural cell adhesion molecule NCAM is directly involved in promoting neurite outgrowth from cultured neural retinal cells
    • Sandig M., Rao Y., Siu C.-H. The homophilic binding site of the neural cell adhesion molecule NCAM is directly involved in promoting neurite outgrowth from cultured neural retinal cells. J. Biol. Chem. 269:1994;14841-14848.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14841-14848
    • Sandig, M.1    Rao, Y.2    Siu, C.-H.3
  • 47
    • 0037025359 scopus 로고    scopus 로고
    • Induction of neuronal differentiation by a peptide corresponding to the homophilic binding site of the second Ig module of NCAM
    • Soroka V., Kiryushko D., Novitskaya V., Rønn L.C., Poulsen F.M., Holm A., Bock E., Berezin V. Induction of neuronal differentiation by a peptide corresponding to the homophilic binding site of the second Ig module of NCAM. J. Biol. Chem. 227:2002;24676-24683.
    • (2002) J. Biol. Chem. , vol.227 , pp. 24676-24683
    • Soroka, V.1    Kiryushko, D.2    Novitskaya, V.3    Rønn, L.C.4    Poulsen, F.M.5    Holm, A.6    Bock, E.7    Berezin, V.8
  • 48
    • 0032516658 scopus 로고    scopus 로고
    • Crystal structure of hemolin: A horseshoe shape with implications for homophilic adhesion
    • Su X.-D., Gastinel L.N., Vaughn D.E., Faye I., Poon P., Bjorkman P.J. Crystal structure of hemolin. a horseshoe shape with implications for homophilic adhesion Science. 281:1998;991-995.
    • (1998) Science , vol.281 , pp. 991-995
    • Su, X.-D.1    Gastinel, L.N.2    Vaughn, D.E.3    Faye, I.4    Poon, P.5    Bjorkman, P.J.6
  • 49
    • 0032953786 scopus 로고    scopus 로고
    • E-cadherin functions as a cis-dimer at the cell-cell adhesive interface in vivo
    • Takeda H., Shimoyama Y., Nagafuchi A., Hirohashi S. E-cadherin functions as a cis-dimer at the cell-cell adhesive interface in vivo. Nat. Struct. Biol. 6:1999;310-312.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 310-312
    • Takeda, H.1    Shimoyama, Y.2    Nagafuchi, A.3    Hirohashi, S.4
  • 50
    • 0027730439 scopus 로고
    • Genetic deletion of a neural cell adhesion molecule variant (NCAM-180) produces defects in the central nervous system
    • Tomasiewicz H., Ono K., Yee D., Thompson C., Goridis C., Rutishauser U., Magnuson T. Genetic deletion of a neural cell adhesion molecule variant (NCAM-180) produces defects in the central nervous system. Neuron. 11:1993;1163-1174.
    • (1993) Neuron , vol.11 , pp. 1163-1174
    • Tomasiewicz, H.1    Ono, K.2    Yee, D.3    Thompson, C.4    Goridis, C.5    Rutishauser, U.6    Magnuson, T.7
  • 51
    • 0029123586 scopus 로고
    • PC12-E2 cells: A stable variant with altered responses to growth factor stimulation
    • Wu Y.Y., Bradshaw R.A. PC12-E2 cells. a stable variant with altered responses to growth factor stimulation J. Cell. Physiol. 164:1995;522-532.
    • (1995) J. Cell. Physiol. , vol.164 , pp. 522-532
    • Wu, Y.Y.1    Bradshaw, R.A.2
  • 52
    • 0030911709 scopus 로고    scopus 로고
    • Dimeric association and segmental variability in the structure of human CD4
    • Wu H., Kwong P.D., Hendrickson W.A. Dimeric association and segmental variability in the structure of human CD4. Nature. 387:1997;527-530.
    • (1997) Nature , vol.387 , pp. 527-530
    • Wu, H.1    Kwong, P.D.2    Hendrickson, W.A.3


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