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Volumn 10, Issue 10, 2003, Pages 843-848

The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; GLYCOPROTEIN; INTEGRIN; LIGAND; PROTEIN SEMA4D; SEMAPHORIN; UNCLASSIFIED DRUG;

EID: 0141507038     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb977     Document Type: Article
Times cited : (144)

References (46)
  • 1
    • 0027787683 scopus 로고
    • The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules
    • Kolodkin, A.L., Matthes, D.J. & Goodman, C.S. The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules. Cell 75, 1389-1399 (1993).
    • (1993) Cell , vol.75 , pp. 1389-1399
    • Kolodkin, A.L.1    Matthes, D.J.2    Goodman, C.S.3
  • 2
    • 0000969241 scopus 로고    scopus 로고
    • Unified nomenclature for the semaphorins/collapsins
    • Semaphorin Nomenclature Committee (S.N.). Unified nomenclature for the semaphorins/collapsins. Cell 97, 551-552 (1999).
    • (1999) Cell , vol.97 , pp. 551-552
  • 3
    • 0027373701 scopus 로고
    • Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
    • Luo, Y., Raible, D. & Raper, J.A. Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. Cell 75, 217-227 (1993).
    • (1993) Cell , vol.75 , pp. 217-227
    • Luo, Y.1    Raible, D.2    Raper, J.A.3
  • 4
    • 0033956733 scopus 로고    scopus 로고
    • Semaphorins and their receptors in vertebrates and invertebrates
    • Raper, J.A. Semaphorins and their receptors in vertebrates and invertebrates. Curr. Opin. Neurobiol. 10, 88-94 (2000).
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 88-94
    • Raper, J.A.1
  • 5
    • 0033214312 scopus 로고    scopus 로고
    • Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors
    • Takahashi, T. et al. Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors. Cell 99, 59-69 (1999).
    • (1999) Cell , vol.99 , pp. 59-69
    • Takahashi, T.1
  • 6
    • 20244364929 scopus 로고    scopus 로고
    • Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
    • Tamagnone, L. et al. Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates. Cell 99, 71-80 (1999).
    • (1999) Cell , vol.99 , pp. 71-80
    • Tamagnone, L.1
  • 7
    • 0030847193 scopus 로고    scopus 로고
    • Neuropilin is a receptor for the axonal chemorepellent Semaphorin III
    • He, Z. & Tessier-Lavigne, M. Neuropilin is a receptor for the axonal chemorepellent Semaphorin III. Cell 90, 739-751 (1997).
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 8
    • 0030829388 scopus 로고    scopus 로고
    • Neuropilin is a semaphorin III receptor
    • Kolodkin, A.L. et al. Neuropilin is a semaphorin III receptor. Cell 90, 753-762 (1997).
    • (1997) Cell , vol.90 , pp. 753-762
    • Kolodkin, A.L.1
  • 9
    • 0032433853 scopus 로고    scopus 로고
    • Plexin A is a neuronal semaphorin receptor that controls axon guidance
    • Winberg, M.L. et al. Plexin A is a neuronal semaphorin receptor that controls axon guidance. Cell 95, 903-916 (1998).
    • (1998) Cell , vol.95 , pp. 903-916
    • Winberg, M.L.1
  • 10
    • 0001290687 scopus 로고    scopus 로고
    • Domains in plexins: Links to integrins and transcription factors
    • Bork, P., Doerks, T., Springer, T.A. & Snel, B. Domains in plexins: links to integrins and transcription factors. Trends Biochem. Sci. 24, 261-263 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 261-263
    • Bork, P.1    Doerks, T.2    Springer, T.A.3    Snel, B.4
  • 11
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ 3
    • Xiong, J.P. et al. Crystal structure of the extracellular segment of integrin αVβ3. Science 294, 339-345 (2001).
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1
  • 12
    • 0029976874 scopus 로고    scopus 로고
    • Human CD100, a novel leukocyte semaphorin that promotes B-cell aggregation and differentiation
    • Hall, K.T. et al. Human CD100, a novel leukocyte semaphorin that promotes B-cell aggregation and differentiation. Proc. Natl. Acad. Sci. USA 93, 11780-11785 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11780-11785
    • Hall, K.T.1
  • 13
    • 0033634849 scopus 로고    scopus 로고
    • The class IV semaphorin CD100 plays nonredundant roles in the immune system: Defective B and T cell activation in CD100-deficient mice
    • Shi, W. et al. The class IV semaphorin CD100 plays nonredundant roles in the immune system: defective B and T cell activation in CD100-deficient mice. Immunity 13, 633-642 (2000).
    • (2000) Immunity , vol.13 , pp. 633-642
    • Shi, W.1
  • 14
    • 0033636321 scopus 로고    scopus 로고
    • Identification of CD72 as a lymphocyte receptor for the class IV semaphorin CD100: A novel mechanism for regulating B cell signaling
    • Kumanogoh, A. et al. Identification of CD72 as a lymphocyte receptor for the class IV semaphorin CD100: a novel mechanism for regulating B cell signaling. Immunity 13, 621-631 (2000).
    • (2000) Immunity , vol.13 , pp. 621-631
    • Kumanogoh, A.1
  • 15
    • 0036711644 scopus 로고    scopus 로고
    • The semaphorin 4D receptor controls invasive growth by coupling with Met
    • Giordano, S. et al. The semaphorin 4D receptor controls invasive growth by coupling with Met. Nat. Cell. Biol. 4, 720-724 (2002).
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 720-724
    • Giordano, S.1
  • 16
    • 0034660088 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast
    • Sprague, E.R., Redd, M.J., Johnson, A.D. & Wolberger, C. Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast. EMBO J. 19, 3016-3027 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3016-3027
    • Sprague, E.R.1    Redd, M.J.2    Johnson, A.D.3    Wolberger, C.4
  • 17
    • 0029593456 scopus 로고
    • The structure of the G protein heterotrimer Gi α1 β1 γ 2
    • Wall, M.A. et al. The structure of the G protein heterotrimer Gi α1 β1 γ2. Cell 83, 1047-1058 (1995).
    • (1995) Cell , vol.83 , pp. 1047-1058
    • Wall, M.A.1
  • 18
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein βγ dimer at 2.1 Å resolution
    • Sondek, J., Bohm, A., Lambright, D.G., Hamm, H.E. & Sigler, P.B. Crystal structure of a G-protein βγ dimer at 2.1 Å resolution. Nature 379, 369-374 (1996).
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 19
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
    • Stuart, D.I., Levine, M., Muirhead, H. & Stammers, D.K. Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å. J. Mol. Biol. 134, 109-142 (1979).
    • (1979) J. Mol. Biol. , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 20
    • 0026035170 scopus 로고
    • Assignment of disulphide bonds in human platelet GPIIIa. A disulphide pattern for the β-subunits of the integrin family
    • Calvete, J.J., Henschen, A. & Gonzalez-Rodriguez, J. Assignment of disulphide bonds in human platelet GPIIIa. A disulphide pattern for the β-subunits of the integrin family. Biochem. J. 274, 63-71 (1991).
    • (1991) Biochem. J. , vol.274 , pp. 63-71
    • Calvete, J.J.1    Henschen, A.2    Gonzalez-Rodriguez, J.3
  • 21
    • 0033539598 scopus 로고    scopus 로고
    • Semaphorin 3A growth cone collapse requires a sequence homologous to tarantula hanatoxin
    • Behar, O., Mizuno, K., Badminton, M. & Woolf, C.J. Semaphorin 3A growth cone collapse requires a sequence homologous to tarantula hanatoxin. Proc. Natl. Acad. Sci. USA 96, 13501-13505 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13501-13505
    • Behar, O.1    Mizuno, K.2    Badminton, M.3    Woolf, C.J.4
  • 22
    • 0032571382 scopus 로고    scopus 로고
    • The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization
    • Klostermann, A., Lohrum, M., Adams, R.H. & Puschel, A.W. The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization. J. Biol. Chem. 273, 7326-7331 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 7326-7331
    • Klostermann, A.1    Lohrum, M.2    Adams, R.H.3    Puschel, A.W.4
  • 23
    • 0032546965 scopus 로고    scopus 로고
    • Collapsin-1 covalently dimerizes, and dimerization is necessary for collapsing activity
    • Koppel, A.M. & Raper, J.A. Collapsin-1 covalently dimerizes, and dimerization is necessary for collapsing activity. J. Biol. Chem. 273, 15708-15713 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15708-15713
    • Koppel, A.M.1    Raper, J.A.2
  • 24
    • 0030886550 scopus 로고    scopus 로고
    • A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members
    • Koppel, A.M., Feiner, L., Kobayashi, H. & Raper, J.A. A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members. Neuron 19, 531-537 (1997).
    • (1997) Neuron , vol.19 , pp. 531-537
    • Koppel, A.M.1    Feiner, L.2    Kobayashi, H.3    Raper, J.A.4
  • 25
    • 0032475963 scopus 로고    scopus 로고
    • Supersites within superfolds. Binding site similarity in the absence of homology
    • Russell, R.B., Sasieni, P.D. & Sternberg, M.J. Supersites within superfolds. Binding site similarity in the absence of homology. J. Mol. Biol. 282, 903-918 (1998).
    • (1998) J. Mol. Biol. , vol.282 , pp. 903-918
    • Russell, R.B.1    Sasieni, P.D.2    Sternberg, M.J.3
  • 26
    • 0037320703 scopus 로고    scopus 로고
    • Semaphorin junction: Making tracks toward neural connectivity
    • Pasterkamp, R.J. & Kolodkin, A.L. Semaphorin junction: making tracks toward neural connectivity. Curr. Opin. Neurobiol. 13, 79-89 (2003).
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 79-89
    • Pasterkamp, R.J.1    Kolodkin, A.L.2
  • 27
    • 0035748337 scopus 로고    scopus 로고
    • Platelet integrin αIIbβ3-ligand interactions: What can we learn from the structure?
    • Kamata, T. & Takada, Y. Platelet integrin αIIbβ3-ligand interactions: what can we learn from the structure? Int. J. Hematol. 74, 382-389 (2001).
    • (2001) Int. J. Hematol. , vol.74 , pp. 382-389
    • Kamata, T.1    Takada, Y.2
  • 28
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin α Vβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J.P. et al. Crystal structure of the extracellular segment of integrin α Vβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155 (2002).
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1
  • 29
    • 0025372845 scopus 로고
    • High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants
    • Davis, S.J. et al. High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants. J. Biol. Chem. 265, 10410-10418 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 10410-10418
    • Davis, S.J.1
  • 30
    • 0019493512 scopus 로고
    • Selection of specific wheat germ agglutinin-resistant (WgaR) phenotypes from Chinese hamster ovary cell populations containing numerous lecR genotypes
    • Stanley, P. Selection of specific wheat germ agglutinin-resistant (WgaR) phenotypes from Chinese hamster ovary cell populations containing numerous lecR genotypes. Mol. Cell Biol. 1, 687-696 (1981).
    • (1981) Mol. Cell Biol. , vol.1 , pp. 687-696
    • Stanley, P.1
  • 31
    • 0030998531 scopus 로고    scopus 로고
    • Expression, crystallization, and preliminary X-ray analysis of a sialic acid-binding fragment of sialoadhesin in the presence and absence of ligand
    • May, A.P. et al. Expression, crystallization, and preliminary X-ray analysis of a sialic acid-binding fragment of sialoadhesin in the presence and absence of ligand. Protein Sci. 6, 717-721 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 717-721
    • May, A.P.1
  • 32
    • 0035073966 scopus 로고    scopus 로고
    • Crystallization and functional analysis of a soluble deglycosylated form of the human costimulatory molecule B7-1
    • Davis, S.J. et al. Crystallization and functional analysis of a soluble deglycosylated form of the human costimulatory molecule B7-1. Acta Crystallogr. D 57, 605-608 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 605-608
    • Davis, S.J.1
  • 33
    • 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, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB version 2.0
    • Weeks, C.M. & Miller, R. The design and implementation of SnB version 2.0. J. Appl. Crystallogr. 32, 120-124 (1999).
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 37
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger, T.C. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. D 59, 38-44 (2003).
    • (2003) Acta Crystallogr. D , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 38
    • 0037242985 scopus 로고    scopus 로고
    • Automated side-chain model building and sequence assignment by template matching
    • Terwilliger, T.C. Automated side-chain model building and sequence assignment by template matching. Acta Crystallogr. D 59, 45-49 (2003).
    • (2003) Acta Crystallogr. D , vol.59 , pp. 45-49
    • Terwilliger, T.C.1
  • 39
    • 84889120137 scopus 로고
    • Improved methods of the building of proteins 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 of the building of proteins models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 41
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan, K.D. & Zhang, K.Y. Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72, 245-270 (1999).
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 42
    • 0036077402 scopus 로고    scopus 로고
    • ARP/wARP's model-building algorithms. I. The main chain
    • Morris, R.J., Perrakis, A. & Lamzin, V.S. ARP/wARP's model-building algorithms. I. The main chain. Acta Crystallogr. D 58, 968-975 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 968-975
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 43
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza, J. Implementation of molecular replacement in AMoRe. Acta Crystallogr. D 57, 1367-1372 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 44
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D 55, 938-940 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 45
    • 0035923529 scopus 로고    scopus 로고
    • Inhibition of lung cancer cell growth and induction of apoptosis after reexpression of 3p21.3 candidate tumor suppressor gene SEMA3B
    • Tomizawa, Y. et al. Inhibition of lung cancer cell growth and induction of apoptosis after reexpression of 3p21.3 candidate tumor suppressor gene SEMA3B. Proc. Natl. Acad. Sci. USA 98, 13954-13959 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13954-13959
    • Tomizawa, Y.1
  • 46
    • 0029871193 scopus 로고    scopus 로고
    • Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p 21, a region deleted in lung cancer
    • Xiang, R.H. et al. Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer. Genomics 32, 39-48 (1996).
    • (1996) Genomics , vol.32 , pp. 39-48
    • Xiang, R.H.1


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