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Volumn 64, Issue 3, 2006, Pages 665-672

Solution structures of the first and fourth TSR domains of F-spondin

Author keywords

Extracellular matrix; F spondin; Neuron development; NMR structure; TSR

Indexed keywords

ARGININE; DISULFIDE; F SPONDIN; SCLEROPROTEIN; THROMBOSPONDIN; THROMBOSPONDIN 1; THROMBOSPONDIN 4; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 33746268448     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21030     Document Type: Article
Times cited : (32)

References (55)
  • 1
    • 0026770381 scopus 로고
    • F-spondin: A gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neurite extension
    • Klar A, Baldassare M, Jessell TM. F-spondin: a gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neurite extension. Cell 1992;69: 95-110.
    • (1992) Cell , vol.69 , pp. 95-110
    • Klar, A.1    Baldassare, M.2    Jessell, T.M.3
  • 2
    • 0027295651 scopus 로고
    • Ectopic neural expression of a floor plate marker in frog embryos injected with the midline transcription factor Pintallavis
    • Ruiz i Altaba A, Cox C, Jessell TM, Klar A. Ectopic neural expression of a floor plate marker in frog embryos injected with the midline transcription factor Pintallavis. Proc Natl Acad Sci USA 1993;90:8268-8272.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8268-8272
    • Ruiz, I.1    Altaba, A.2    Cox, C.3    Jessell, T.M.4    Klar, A.5
  • 3
    • 16544366593 scopus 로고    scopus 로고
    • The neuronal class 2 TSR proteins F-spondin and Mindin: A small family with divergent biological activities
    • Feinstein Y, Klar A. The neuronal class 2 TSR proteins F-spondin and Mindin: a small family with divergent biological activities. Int J Biochem Cell Biol 2004;36:975-980.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 975-980
    • Feinstein, Y.1    Klar, A.2
  • 5
    • 0027257941 scopus 로고
    • A single chain 19-kDa fragment from bovine thrombospondin binds to type V collagen and heparin
    • Takagi J, Fujisawa T, Usui T, Aoyama T, Saito Y. A single chain 19-kDa fragment from bovine thrombospondin binds to type V collagen and heparin. J Biol Chem 1993;268:15544-15549.
    • (1993) J Biol Chem , vol.268 , pp. 15544-15549
    • Takagi, J.1    Fujisawa, T.2    Usui, T.3    Aoyama, T.4    Saito, Y.5
  • 6
    • 0027415981 scopus 로고
    • Inhibition of fibronectin binding and fibronectin-mediated cell adhesion to collagen by a peptide from the second type I repeat of thrombospondin
    • Sipes JM, Guo N, Negre E, Vogel T, Krutzsch HC, Roberts DD. Inhibition of fibronectin binding and fibronectin-mediated cell adhesion to collagen by a peptide from the second type I repeat of thrombospondin. J Cell Biol 1993;121:469-477.
    • (1993) J Cell Biol , vol.121 , pp. 469-477
    • Sipes, J.M.1    Guo, N.2    Negre, E.3    Vogel, T.4    Krutzsch, H.C.5    Roberts, D.D.6
  • 9
    • 0026673905 scopus 로고
    • Heparin-binding peptides from the type I repeats of thrombospondin: Structural requirements for heparin binding and promotion of melanoma cell adhesion and chemotaxis
    • Guo NH, Krutzsch HC, Negre E, Zabrenetzky VS, Roberts DD. Heparin-binding peptides from the type I repeats of thrombospondin: structural requirements for heparin binding and promotion of melanoma cell adhesion and chemotaxis. J Biol Chem 1992;267:19349-19355.
    • (1992) J Biol Chem , vol.267 , pp. 19349-19355
    • Guo, N.H.1    Krutzsch, H.C.2    Negre, E.3    Zabrenetzky, V.S.4    Roberts, D.D.5
  • 10
    • 0030739102 scopus 로고    scopus 로고
    • Cell adhesion to a motif shared by the malaria circumsporozoite protein and thrombospondin is mediated by its glycosaminoglycan-binding region and not by CSVTCG
    • Gantt SM, Clavijo P, Bai X, Esko JD, Sinnis P. Cell adhesion to a motif shared by the malaria circumsporozoite protein and thrombospondin is mediated by its glycosaminoglycan-binding region and not by CSVTCG. J Biol Chem 1997;272:19205-19213.
    • (1997) J Biol Chem , vol.272 , pp. 19205-19213
    • Gantt, S.M.1    Clavijo, P.2    Bai, X.3    Esko, J.D.4    Sinnis, P.5
  • 11
    • 0033151663 scopus 로고    scopus 로고
    • F-Spondin is required for accurate pathfinding of commissural axons at the floor plate
    • Burstyn-Cohen T, Tzarfaty V, Frumkin A, Feinstein Y, Stoeckli E, Klar A. F-Spondin is required for accurate pathfinding of commissural axons at the floor plate. Neuron 1999;23:233-246.
    • (1999) Neuron , vol.23 , pp. 233-246
    • Burstyn-Cohen, T.1    Tzarfaty, V.2    Frumkin, A.3    Feinstein, Y.4    Stoeckli, E.5    Klar, A.6
  • 12
    • 0035836639 scopus 로고    scopus 로고
    • F-spondin is a contact-repellent molecule for embryonic motor neurons
    • Tzarfati-Majar V, Burstyn-Cohen T, Klar A. F-spondin is a contact-repellent molecule for embryonic motor neurons. Proc Natl Acad Sci USA 2001;98:4722-4727.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4722-4727
    • Tzarfati-Majar, V.1    Burstyn-Cohen, T.2    Klar, A.3
  • 13
    • 0032211047 scopus 로고    scopus 로고
    • Accumulation of F-spondin in injured peripheral nerve promotes the outgrowth of sensory axons
    • Burstyn-Cohen T, Frumkin A, Xu YT, Scherer SS, Klar A. Accumulation of F-spondin in injured peripheral nerve promotes the outgrowth of sensory axons. J Neurosci 1998;18:8875-8885.
    • (1998) J Neurosci , vol.18 , pp. 8875-8885
    • Burstyn-Cohen, T.1    Frumkin, A.2    Xu, Y.T.3    Scherer, S.S.4    Klar, A.5
  • 14
    • 0035371035 scopus 로고    scopus 로고
    • Isolation and characterization of vascular smooth muscle cell growth promoting factor from bovine ovarian follicular fluid and its cDNA cloning from bovine and human ovary
    • Miyamoto K, Morishita Y, Yamazaki M, Minamino N, Kangawa K, Matsuo H, Mizutani T, Yamada K, Minegishi T. Isolation and characterization of vascular smooth muscle cell growth promoting factor from bovine ovarian follicular fluid and its cDNA cloning from bovine and human ovary. Arch Biochem Biophys 2001;390: 93-100.
    • (2001) Arch Biochem Biophys , vol.390 , pp. 93-100
    • Miyamoto, K.1    Morishita, Y.2    Yamazaki, M.3    Minamino, N.4    Kangawa, K.5    Matsuo, H.6    Mizutani, T.7    Yamada, K.8    Minegishi, T.9
  • 15
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-β precursor protein: A candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage
    • Ho A, Südhof TC. Binding of F-spondin to amyloid-β precursor protein: A candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage. Proc Natl Acad Sci USA 2004;101:2548-2553.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2548-2553
    • Ho, A.1    Südhof, T.C.2
  • 16
    • 0023035074 scopus 로고
    • The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins
    • Lawler J, Hynes RO. The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J Cell Biol 1986;103: 1635-1648.
    • (1986) J Cell Biol , vol.103 , pp. 1635-1648
    • Lawler, J.1    Hynes, R.O.2
  • 18
    • 0031573941 scopus 로고    scopus 로고
    • Mindin/F-spondin family: Novel ECM proteins expressed in the zebrafish embryonic axis
    • Higashijima S, Nose A, Eguchi G, Hotta Y, Okamoto H. Mindin/F-spondin family: novel ECM proteins expressed in the zebrafish embryonic axis. Dev Biol 1997;192:211-227.
    • (1997) Dev Biol , vol.192 , pp. 211-227
    • Higashijima, S.1    Nose, A.2    Eguchi, G.3    Hotta, Y.4    Okamoto, H.5
  • 19
    • 0030857354 scopus 로고    scopus 로고
    • M-spondin, a novel ECM protein highly homologous to vertebrate F-spondin, is localized at the muscle attachment sites in the Drosophila embryo
    • Umemiya T, Takeichi M, Nose A. M-spondin, a novel ECM protein highly homologous to vertebrate F-spondin, is localized at the muscle attachment sites in the Drosophila embryo. Dev Biol 1997;186:165-176.
    • (1997) Dev Biol , vol.186 , pp. 165-176
    • Umemiya, T.1    Takeichi, M.2    Nose, A.3
  • 21
    • 0028940096 scopus 로고
    • A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
    • D'Arcangelo G, Miao GG, Chen SC, Soares HD, Morgan JI, Curran T. A protein related to extracellular matrix proteins deleted in the mouse mutant reeler. Nature 1995;374:719-723.
    • (1995) Nature , vol.374 , pp. 719-723
    • D'Arcangelo, G.1    Miao, G.G.2    Chen, S.C.3    Soares, H.D.4    Morgan, J.I.5    Curran, T.6
  • 24
    • 0025087029 scopus 로고
    • Cell-adhesive motif in region II of malarial circumsporozoite protein
    • Rich KA, George FWt, Law JL, Martin WJ. Cell-adhesive motif in region II of malarial circumsporozoite protein. Science 1990;249: 1574-1577.
    • (1990) Science , vol.249 , pp. 1574-1577
    • Rich, K.A.1    George, F.2    Law, J.L.3    Martin, W.J.4
  • 25
  • 26
    • 0040735688 scopus 로고    scopus 로고
    • Heparin-binding growth-associated molecule contains two heparin-binding β-sheet domains that are homologous to the thrombospondin type I repeats
    • Kilpeläinen I, Kaksonen M, Avikainen H, Fath M, Linhardt RJ, Raulo E, Rauvala H. Heparin-binding growth-associated molecule contains two heparin-binding β-sheet domains that are homologous to the thrombospondin type I repeats. J Biol Chem 2000;275: 13564-13570.
    • (2000) J Biol Chem , vol.275 , pp. 13564-13570
    • Kilpeläinen, I.1    Kaksonen, M.2    Avikainen, H.3    Fath, M.4    Linhardt, R.J.5    Raulo, E.6    Rauvala, H.7
  • 27
    • 0033080746 scopus 로고    scopus 로고
    • Peptide mapping and disulfide bond analysis of myeloid progenitor inhibitory chemokine and keratinocyte growth factor by matrix-assisted laser desorption ionization mass spectrometry
    • Navale V, Kaushal P, Hunt S, Burducea I, Gentz R, Khan F, Vertes A. Peptide mapping and disulfide bond analysis of myeloid progenitor inhibitory chemokine and keratinocyte growth factor by matrix-assisted laser desorption ionization mass spectrometry. Anal Biochem 1999;267:125-134.
    • (1999) Anal Biochem , vol.267 , pp. 125-134
    • Navale, V.1    Kaushal, P.2    Hunt, S.3    Burducea, I.4    Gentz, R.5    Khan, F.6    Vertes, A.7
  • 30
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Progr NMR Spectr 1999;34:93-158.
    • (1999) Progr NMR Spectr , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 31
    • 0036360446 scopus 로고    scopus 로고
    • Intraresidual HNCA: An experiment for correlating only intraresidual backbone resonances
    • Permi P. Intraresidual HNCA: an experiment for correlating only intraresidual backbone resonances. J Biomol NMR 2002;23:201-209.
    • (2002) J Biomol NMR , vol.23 , pp. 201-209
    • Permi, P.1
  • 32
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 1994;4:845-858.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 36
    • 0034923123 scopus 로고    scopus 로고
    • Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data
    • Moseley HN, Monleon D, Montelione GT. Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol 2001; 339:91-108.
    • (2001) Methods Enzymol , vol.339 , pp. 91-108
    • Moseley, H.N.1    Monleon, D.2    Montelione, G.T.3
  • 37
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 1997;273:283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 38
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 2002;319:209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 39
    • 4344698912 scopus 로고    scopus 로고
    • Automated NMR protein structure calculation
    • Güntert P. Automated NMR protein structure calculation. Prog NMRes Spectr 2003;43:105-125.
    • (2003) Prog NMRes Spectr , vol.43 , pp. 105-125
    • Güntert, P.1
  • 41
    • 0030236215 scopus 로고    scopus 로고
    • The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules
    • Luginbühl P, Güntert P, Billeter M, Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J Biomol NMR 1996;8: 136-146.
    • (1996) J Biomol NMR , vol.8 , pp. 136-146
    • Luginbühl, P.1    Güntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 42
    • 0034140558 scopus 로고    scopus 로고
    • Point-centered domain decomposition for parallel molecular dynamics simulation
    • Koradi R, Billeter M, Güntert P. Point-centered domain decomposition for parallel molecular dynamics simulation. Comput Phys Commun 2000;124:139-147.
    • (2000) Comput Phys Commun , vol.124 , pp. 139-147
    • Koradi, R.1    Billeter, M.2    Güntert, P.3
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55, 29-32.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 44
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • 13C NMR chemical shifts can predict disulfide bond formation. J Biomol NMR 2000;18:165-171.
    • (2000) J Biomol NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 46
    • 0034577985 scopus 로고    scopus 로고
    • Protein C-mannosylation: Facts and questions
    • Furmanek A, Hofsteenge J. Protein C-mannosylation: facts and questions. Acta Biochim Pol 2000;47:781-789.
    • (2000) Acta Biochim Pol , vol.47 , pp. 781-789
    • Furmanek, A.1    Hofsteenge, J.2
  • 47
    • 27144504391 scopus 로고    scopus 로고
    • F-spondin interaction with the apolipoprotein e receptor ApoEr2 affects processing of amyloid precursor protein
    • Hoe HS, Wessner D, Beffert U, Becker AG, Matsuoka Y, Rebeck GW. F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein. Mol Cell Biol 2005;25:9259-9268.
    • (2005) Mol Cell Biol , vol.25 , pp. 9259-9268
    • Hoe, H.S.1    Wessner, D.2    Beffert, U.3    Becker, A.G.4    Matsuoka, Y.5    Rebeck, G.W.6
  • 48
    • 0029020912 scopus 로고
    • Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor
    • Daly NL, Scanlon MJ, Djordjevic JT, Kroon PA, Smith R. Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor. Proc Natl Acad Sci USA 1995;92: 6334-6338.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6334-6338
    • Daly, N.L.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 49
    • 0028866813 scopus 로고
    • Three-dimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor
    • Daly NL, Djordjevic JT, Kroon PA, Smith R. Three-dimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor. Biochemistry 1995;34:14474-14481.
    • (1995) Biochemistry , vol.34 , pp. 14474-14481
    • Daly, N.L.1    Djordjevic, J.T.2    Kroon, P.A.3    Smith, R.4
  • 50
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
    • Fass D, Blacklow S, Kim PS, Berger JM. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature 1997;388:691-693.
    • (1997) Nature , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.S.3    Berger, J.M.4
  • 51
    • 0035909826 scopus 로고    scopus 로고
    • Calcium coordination and pH dependence of the calcium affinity of ligand-binding repeat CR7 from the LRP: Comparison with related domains from the LRP and the LDL receptor
    • Simonovic M, Dolmer K, Huang W, Strickland DK, Volz K, Gettins PG. Calcium coordination and pH dependence of the calcium affinity of ligand-binding repeat CR7 from the LRP: comparison with related domains from the LRP and the LDL receptor. Biochemistry 2001;40:15127-15134.
    • (2001) Biochemistry , vol.40 , pp. 15127-15134
    • Simonovic, M.1    Dolmer, K.2    Huang, W.3    Strickland, D.K.4    Volz, K.5    Gettins, P.G.6
  • 52
    • 2342648870 scopus 로고    scopus 로고
    • X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein
    • Verdaguer N, Fita I, Reithmayer M, Moser R, Blaas D. X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein. Nat Struct Mol Biol 2004;11:429-434.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 429-434
    • Verdaguer, N.1    Fita, I.2    Reithmayer, M.3    Moser, R.4    Blaas, D.5
  • 54
    • 22244478077 scopus 로고    scopus 로고
    • Structure and physiologic function of the low-density lipoprotein receptor
    • Jeon H, Blacklow SC. Structure and physiologic function of the low-density lipoprotein receptor. Annu Rev Biochem 2005;74:535-562.
    • (2005) Annu Rev Biochem , vol.74 , pp. 535-562
    • Jeon, H.1    Blacklow, S.C.2
  • 55
    • 0030065240 scopus 로고    scopus 로고
    • Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor
    • Mer G, Hietter H, Lefevre JF. Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nat Struct Biol 1996;3:45-53.
    • (1996) Nat Struct Biol , vol.3 , pp. 45-53
    • Mer, G.1    Hietter, H.2    Lefevre, J.F.3


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