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Volumn 26, Issue , 1997, Pages 259-288

Modular peptide recognition domains in eukaryotic signaling

Author keywords

PDZ; PTB; SH2; SH3; Src homology; Tyrosine kinase

Indexed keywords

PEPTIDE; PHOSPHATASE; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; TYROSINE;

EID: 0030950608     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.26.1.259     Document Type: Review
Times cited : (477)

References (104)
  • 1
    • 0028838133 scopus 로고
    • SH3 domains specifically regulate kinase activity of expressed Src family proteins
    • Abrams CS, Zhao W. 1995. SH3 domains specifically regulate kinase activity of expressed Src family proteins. J. Biol. Chem. 270:333-39
    • (1995) J. Biol. Chem. , vol.270 , pp. 333-339
    • Abrams, C.S.1    Zhao, W.2
  • 2
    • 0029766101 scopus 로고    scopus 로고
    • Coordinate activation of c-Src by SH3-and SH2-binding sites on a novel p130Cas-related protein, Sin
    • Alexandropoulos K, Baltimore D. 1996. Coordinate activation of c-Src by SH3-and SH2-binding sites on a novel p130Cas-related protein, Sin. Genes Dev. 10:1341-55
    • (1996) Genes Dev. , vol.10 , pp. 1341-1355
    • Alexandropoulos, K.1    Baltimore, D.2
  • 3
    • 0028568639 scopus 로고
    • A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
    • Blaikie P, Immanuel D, Wu J, Li N, Yajnik V, Margolis B. 1994. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269:32031-34
    • (1994) J. Biol. Chem. , vol.269 , pp. 32031-32034
    • Blaikie, P.1    Immanuel, D.2    Wu, J.3    Li, N.4    Yajnik, V.5    Margolis, B.6
  • 4
    • 0026665009 scopus 로고
    • Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3-OH kinase
    • Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, et al. 1992. Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3-OH kinase. Nature 358:684-87
    • (1992) Nature , vol.358 , pp. 684-687
    • Booker, G.W.1    Breeze, A.L.2    Downing, A.K.3    Panayotou, G.4    Gout, I.5
  • 5
    • 0022450133 scopus 로고
    • Amino-aromatic interactions in proteins
    • Burley SK, Petsko GA. 1986. Amino-aromatic interactions in proteins. FEBS Lett. 203:139-43
    • (1986) FEBS Lett. , vol.203 , pp. 139-143
    • Burley, S.K.1    Petsko, G.A.2
  • 8
    • 0028342948 scopus 로고
    • SH-PTP2 SH2 domain binding specificity is defined by direct interactions with PDGF β-receptor, EGF receptor, and IRS-1 derived phosphopeptides
    • Case RD, Piccione E, Wolf G, Lechleider RJ, Chaudhuri M, et al. 1994. SH-PTP2 SH2 domain binding specificity is defined by direct interactions with PDGF β-receptor, EGF receptor, and IRS-1 derived phosphopeptides. J. Biol. Chem. 269:10467-74
    • (1994) J. Biol. Chem. , vol.269 , pp. 10467-10474
    • Case, R.D.1    Piccione, E.2    Wolf, G.3    Lechleider, R.J.4    Chaudhuri, M.5
  • 10
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of abl and is similar to Bcr and GAP-rho
    • Cicchetti P, Mayer BJ, Theil G, Baltimore D. 1992. Identification of a protein that binds to the SH3 region of abl and is similar to Bcr and GAP-rho. Science 257:803-6
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Theil, G.3    Baltimore, D.4
  • 11
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. 1995. A hot spot of binding energy in a hormone-receptor interface. Science 267:383-86
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 12
    • 0025315794 scopus 로고
    • Tyrosine phosphorylation is a signal for the trafficking of pp85, a polypeptide associated with phosphatidylinositol kinase activity
    • Cohen B, Yoakim M, Piwnica-Worms H, Roberts T, Schaffhausen BS. 1990. Tyrosine phosphorylation is a signal for the trafficking of pp85, a polypeptide associated with phosphatidylinositol kinase activity. Proc. Natl. Acad. Sci. USA 87: 4458-62
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4458-4462
    • Cohen, B.1    Yoakim, M.2    Piwnica-Worms, H.3    Roberts, T.4    Schaffhausen, B.S.5
  • 13
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D. 1995. Modular binding domains in signal transduction proteins. Cell 80:237-48
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 14
    • 0030062879 scopus 로고    scopus 로고
    • Protein structure-based combinatorial chemistry: Discovery of non-peptide binding elements to Src SH3 domain
    • Combs AP, Kapoor TM, Feng S, Chen JK, Daude-Snow LF, Schreiber SL. 1996. Protein structure-based combinatorial chemistry: discovery of non-peptide binding elements to Src SH3 domain. J. Am. Chem. Soc. 118:287-88
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 287-288
    • Combs, A.P.1    Kapoor, T.M.2    Feng, S.3    Chen, J.K.4    Daude-Snow, L.F.5    Schreiber, S.L.6
  • 15
    • 0028807441 scopus 로고
    • Enhanced affinities and specificities of consolidated ligands for the Src homology (SH) 3 and SH2 domains of Abelson protein-tyrosine kinase
    • Cowburn D, Zheng J, Xu Q, Barany G. 1995. Enhanced affinities and specificities of consolidated ligands for the Src homology (SH) 3 and SH2 domains of Abelson protein-tyrosine kinase. J. Biol. Chem. 270:26738-41
    • (1995) J. Biol. Chem. , vol.270 , pp. 26738-26741
    • Cowburn, D.1    Zheng, J.2    Xu, Q.3    Barany, G.4
  • 16
    • 0027965513 scopus 로고
    • Binding of the GRB2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domain for Sos proline-rich motifs
    • Cussac D, Frech M, Chardin P. 1994. Binding of the GRB2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domain for Sos proline-rich motifs. EMBO J. 13:4011-21
    • (1994) EMBO J. , vol.13 , pp. 4011-4021
    • Cussac, D.1    Frech, M.2    Chardin, P.3
  • 17
    • 0027043276 scopus 로고
    • Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene
    • Daniel MD, Kirchoff F, Czajak SC, Sehgal PK, Derosiers RC. 1992. Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene. Science 258:1938-41
    • (1992) Science , vol.258 , pp. 1938-1941
    • Daniel, M.D.1    Kirchoff, F.2    Czajak, S.C.3    Sehgal, P.K.4    Derosiers, R.C.5
  • 18
    • 0028804160 scopus 로고
    • Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients
    • Deacon NJ, Tsykin A, Solomon A, Smith K, Ludford-Menting M, et al. 1995. Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients. Science 270:988-91
    • (1995) Science , vol.270 , pp. 988-991
    • Deacon, N.J.1    Tsykin, A.2    Solomon, A.3    Smith, K.4    Ludford-Menting, M.5
  • 19
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain - Molecular basis of peptide recognition by PDZ domains
    • Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain - molecular basis of peptide recognition by PDZ domains. Cell 85: 1067-76
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 20
    • 0028337397 scopus 로고
    • Crystal structure of the regulatory domains of the Src-family tyrosine kinase lck
    • Eck MJ, Atwell SK, Shoelson SE, Harrison SC. 1994. Crystal structure of the regulatory domains of the Src-family tyrosine kinase lck. Nature 368:764-69
    • (1994) Nature , vol.368 , pp. 764-769
    • Eck, M.J.1    Atwell, S.K.2    Shoelson, S.E.3    Harrison, S.C.4
  • 21
    • 0030010590 scopus 로고    scopus 로고
    • Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor
    • Eck MJ, Dhepaganon S, Trub T, Nolte RT, Shoelson SE. 1996. Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor. Cell 85:695-705
    • (1996) Cell , vol.85 , pp. 695-705
    • Eck, M.J.1    Dhepaganon, S.2    Trub, T.3    Nolte, R.T.4    Shoelson, S.E.5
  • 22
    • 0030066325 scopus 로고    scopus 로고
    • Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
    • Eck MJ, Pluskey S, Trüb T, Harrison SC, Shoelson SE. 1996. Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 379:277-80
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trüb, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 23
    • 0027502504 scopus 로고
    • Recognition of a high affinity phosphotyrosyl peptide by the Src homology 2 domain of p56lck
    • Eck MJ, Shoelson SE, Harrison SC. 1993. Recognition of a high affinity phosphotyrosyl peptide by the Src homology 2 domain of p56lck. Nature 362:87-91
    • (1993) Nature , vol.362 , pp. 87-91
    • Eck, M.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 24
    • 0027411585 scopus 로고
    • SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange
    • Felder S, Zhou M, Hu P, Urena J, Ullrich A, et al. 1993. SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13:1449-55
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1449-1455
    • Felder, S.1    Zhou, M.2    Hu, P.3    Urena, J.4    Ullrich, A.5
  • 25
    • 0027940655 scopus 로고
    • SH2 and SH3 domains as molecular adhesives : The interactions of Crk and Abl
    • Feller SM, Ren R, Hanafusa H, Baltimore D. 1994. SH2 and SH3 domains as molecular adhesives : the interactions of Crk and Abl. Trends Biochem. Sci. 19:453-59
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 453-459
    • Feller, S.M.1    Ren, R.2    Hanafusa, H.3    Baltimore, D.4
  • 26
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng S, Chen JK, Yu H, Simon JA, Schreiber SA. 1994. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266:1241-47
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.A.5
  • 27
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • Feng S, Kasahara C, Rickles RJ, Schreiber SL. 1995. Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc. Natl. Acad. Sci. USA 92:12408-15
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12408-12415
    • Feng, S.1    Kasahara, C.2    Rickles, R.J.3    Schreiber, S.L.4
  • 29
    • 0029645577 scopus 로고
    • The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct
    • Gosser YQ, Zheng J, Overduin M, Mayer BJ, Cowburn D. 1995. The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct. Structure 3:1075-86
    • (1995) Structure , vol.3 , pp. 1075-1086
    • Gosser, Y.Q.1    Zheng, J.2    Overduin, M.3    Mayer, B.J.4    Cowburn, D.5
  • 30
    • 0028675698 scopus 로고
    • NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline rich peptide from Sos
    • Goudreau N, Cornille F, Duchesne M, Parker F, Tocqué B, et al. 1994. NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline rich peptide from Sos. Nature Struct. Biol. 1:898-907
    • (1994) Nature Struct. Biol. , vol.1 , pp. 898-907
    • Goudreau, N.1    Cornille, F.2    Duchesne, M.3    Parker, F.4    Tocqué, B.5
  • 31
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek S, Bax A, Clore GM, Gronenborn AM, Hu J-S, et al. 1996. The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nature Struct. Biol. 3:340-45
    • (1996) Nature Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.-S.5
  • 32
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via novel non-SH2 domain
    • Gustafson TA, He W, Craparo A, Schaub CD, O'Neill TJ. 1995. Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via novel non-SH2 domain. Mol. Cell. Biol. 15:2500-8
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 33
    • 84988043558 scopus 로고
    • Molecular basis for the interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor
    • Hatada MH, Lu X, Laird ER, Green J, Morgenstern JP, et al. 1995. Molecular basis for the interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. Nature 377:32-38
    • (1995) Nature , vol.377 , pp. 32-38
    • Hatada, M.H.1    Lu, X.2    Laird, E.R.3    Green, J.4    Morgenstern, J.P.5
  • 34
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated growth factor receptors
    • Kavanaugh WM, Williams LT. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated growth factor receptors. Science 266:1862-65
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 35
    • 0026664293 scopus 로고
    • GTPase activating protein and phosphatidylinositol 3-kinase bind to a distinct region of the platelet-derived growth factor receptor b subunit
    • Kazlauskas A, Kashishian A, Cooper JA, Valius M. 1992. GTPase activating protein and phosphatidylinositol 3-kinase bind to a distinct region of the platelet-derived growth factor receptor b subunit. Mol. Cell. Biol. 12:2534-44
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2534-2544
    • Kazlauskas, A.1    Kashishian, A.2    Cooper, J.A.3    Valius, M.4
  • 36
    • 0025743306 scopus 로고
    • Importance of the nef gene for maintenance of high virus loads and for development of AIDS
    • Kestler HW III, Ringler DJ, Mori K, Panicali DL, Sehgal PK, et al. 1991. Importance of the nef gene for maintenance of high virus loads and for development of AIDS. Cell 65:651-62
    • (1991) Cell , vol.65 , pp. 651-662
    • Kestler III, H.W.1    Ringler, D.J.2    Mori, K.3    Panicali, D.L.4    Sehgal, P.K.5
  • 38
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor, C3G, bind with unique specificity to the first Src homology 3 domain of Crk
    • Knudsen BS, Feller SM, Hanafusa H. 1994. Four proline-rich sequences of the guanine-nucleotide exchange factor, C3G, bind with unique specificity to the first Src homology 3 domain of Crk. J. Biol. Chem. 269:32781-87
    • (1994) J. Biol. Chem. , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 39
    • 0029066326 scopus 로고
    • Affinity and specificity requirements for the first Src homology 3 domain of the Crk protein
    • Knudsen BS, Zheng J, Feller SM, Mayer JP, Burrell SK, et al. 1995. Affinity and specificity requirements for the first Src homology 3 domain of the Crk protein. EMBO J. 14:2191-98
    • (1995) EMBO J. , vol.14 , pp. 2191-2198
    • Knudsen, B.S.1    Zheng, J.2    Feller, S.M.3    Mayer, J.P.4    Burrell, S.K.5
  • 40
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-50
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 43
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
    • Lee C-H, Kominos D, Jacques S, Margolis B, Schlessinger J, et al. 1994. Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2:423-38
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.-H.1    Kominos, D.2    Jacques, S.3    Margolis, B.4    Schlessinger, J.5
  • 44
    • 0028805516 scopus 로고
    • A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    • Lee C-H, Leung B, Lemmon MA, Zheng J, Cowburn D, et al. 1995. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14:5006-15
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.-H.1    Leung, B.2    Lemmon, M.A.3    Zheng, J.4    Cowburn, D.5
  • 45
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee C-H, Saksela K, Mirza UA, Chait BT, Kuriyan J. 1996. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85:931-42
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.-H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 46
    • 0028303266 scopus 로고
    • Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck
    • Lemmon MA, Ladbury JE. 1994. Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck. Biochemistry 33: 5070-76
    • (1994) Biochemistry , vol.33 , pp. 5070-5076
    • Lemmon, M.A.1    Ladbury, J.E.2
  • 48
    • 0028410481 scopus 로고
    • Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition
    • Lim WA, Richards FM. 1994. Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition. Nature Struct. Biol. 1:221-25
    • (1994) Nature Struct. Biol. , vol.1 , pp. 221-225
    • Lim, W.A.1    Richards, F.M.2
  • 49
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim WA, Richards FM, Fox RO. 1994. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372:375-79
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 50
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias MJ, Hyvönen M, Baraldi E, Schultz J, Sudol M, et al. 1996. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382:646-49
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvönen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5
  • 53
    • 0026601293 scopus 로고
    • Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming ability in vivo
    • Mayer BJ, Jackson PK, Van Etten RA, Baltimore D. 1992. Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming ability in vivo. Mol. Cell. Biol. 12:609-18
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    Van Etten, R.A.3    Baltimore, D.4
  • 55
    • 0025119824 scopus 로고
    • Src homology region 2 domains direct protein-protein interactions in signal transduction
    • Moran MF, Koch CA, Anderson D, Ellis C, England L, et al. 1990. Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl. Acad. Sci. USA 87:8622-26
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8622-8626
    • Moran, M.F.1    Koch, C.A.2    Anderson, D.3    Ellis, C.4    England, L.5
  • 57
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio A, Saraste M, Wilmanns M. 1994. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nature Struct. Biol. 1:546-51
    • (1994) Nature Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 58
    • 0029645589 scopus 로고
    • Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide
    • Narula SS, Yuan RW, Adams SE, Green OM, Green J, et al. 1995. Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptide. Structure 3:1061-73
    • (1995) Structure , vol.3 , pp. 1061-1073
    • Narula, S.S.1    Yuan, R.W.2    Adams, S.E.3    Green, O.M.4    Green, J.5
  • 59
    • 0029878266 scopus 로고    scopus 로고
    • Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes
    • Nolte RT, Eck MJ, Schlessinger J, Shoelson SE, Harrison SC. 1996. Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nature Struct. Biol. 3:364-73
    • (1996) Nature Struct. Biol. , vol.3 , pp. 364-373
    • Nolte, R.T.1    Eck, M.J.2    Schlessinger, J.3    Shoelson, S.E.4    Harrison, S.C.5
  • 60
    • 0026669472 scopus 로고
    • Three-dimensional solution structure of the src homology 2 domain of c-abl
    • Overduin M, Rios CB, Mayer BJ, Baltimore D, Cowburn D. 1992. Three-dimensional solution structure of the src homology 2 domain of c-abl. Cell 70:697-704
    • (1992) Cell , vol.70 , pp. 697-704
    • Overduin, M.1    Rios, C.B.2    Mayer, B.J.3    Baltimore, D.4    Cowburn, D.5
  • 61
    • 0026487847 scopus 로고
    • Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: Structural features and analysis of conformational changes
    • Panayotou G, Bax B, Gout I, Federwisch M, Wroblowski B, et al. 1992. Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J. 11:4261-72
    • (1992) EMBO J. , vol.11 , pp. 4261-4272
    • Panayotou, G.1    Bax, B.2    Gout, I.3    Federwisch, M.4    Wroblowski, B.5
  • 62
    • 0027195236 scopus 로고
    • Interactions between SH2 domains and tyrosine phosphorylated platelet-derived growth factor beta-receptor sequences: Analysis of kinetic parameters by a novel biosensor-based approach
    • Panayotou G, Gish G, End P, Truong O, Gout I, et al. 1993. Interactions between SH2 domains and tyrosine phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach. Mol. Cell. Biol. 13:3567-76
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3567-3576
    • Panayotou, G.1    Gish, G.2    End, P.3    Truong, O.4    Gout, I.5
  • 64
    • 0029142571 scopus 로고
    • Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain-phosphopeptide complex by NMR relaxation, proton exchange and chemical shift approaches
    • Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD. 1995. Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain-phosphopeptide complex by NMR relaxation, proton exchange and chemical shift approaches. Biochemistry 34:11353-62
    • (1995) Biochemistry , vol.34 , pp. 11353-11362
    • Pascal, S.M.1    Yamazaki, T.2    Singer, A.U.3    Kay, L.E.4    Forman-Kay, J.D.5
  • 65
    • 0024246872 scopus 로고
    • Non-catalytic domains of cytoplasmic protein-tyrosine kinases: Regulatory elements in signal transduction
    • Pawson T. 1988. Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction. Oncogene 3:491-95
    • (1988) Oncogene , vol.3 , pp. 491-495
    • Pawson, T.1
  • 66
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. 1995. Protein modules and signalling networks. Nature 373:573-80
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 68
    • 0027336898 scopus 로고
    • Binding kinetics of Lck and Src SH2 domain/phosphopeptide interactions by competition assay and surface plasmon resonance
    • Payne G, Shoelson SE, Gish GD, Pawson T, Walsh CT. 1993. Binding kinetics of Lck and Src SH2 domain/phosphopeptide interactions by competition assay and surface plasmon resonance. Proc. Natl. Acad. Sci. USA 90:4902-6
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4902-4906
    • Payne, G.1    Shoelson, S.E.2    Gish, G.D.3    Pawson, T.4    Walsh, C.T.5
  • 69
  • 70
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren R, Mayer BJ, Cicchetti P, Baltimore D. 1993. Identification of a ten-amino acid proline-rich SH3 binding site. Science 259:1157-61
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 71
    • 0029878111 scopus 로고    scopus 로고
    • pH dependent self-association of the Src homology-2 (SH2) domain of the Src homologous and collagen-like (SHC) protein
    • Rety S, Futterer K, Grucza RA, Munoz CM, Frazier WA, Waksman G. 1996. pH dependent self-association of the Src homology-2 (SH2) domain of the Src homologous and collagen-like (SHC) protein. Protein Sci. 5:405-13
    • (1996) Protein Sci. , vol.5 , pp. 405-413
    • Rety, S.1    Futterer, K.2    Grucza, R.A.3    Munoz, C.M.4    Frazier, W.A.5    Waksman, G.6
  • 72
    • 0028916892 scopus 로고
    • Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein
    • Rosen MK, Yamazaki T, Gish GD, Kay CM, Pawson T, Kay LE. 1995. Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature 374:477-79
    • (1995) Nature , vol.374 , pp. 477-479
    • Rosen, M.K.1    Yamazaki, T.2    Gish, G.D.3    Kay, C.M.4    Pawson, T.5    Kay, L.E.6
  • 73
    • 0025719212 scopus 로고
    • Selective binding of activated pp60 c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60 c-src
    • Roussel RR, Brodeur SR, Shalloway D, Laudano AP. 1991. Selective binding of activated pp60 c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60 c-src. Proc. Natl. Acad. Sci. USA 88:10696-700
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10696-10700
    • Roussel, R.R.1    Brodeur, S.R.2    Shalloway, D.3    Laudano, A.P.4
  • 74
    • 0022977712 scopus 로고
    • A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of fujinami sarcoma virus p130gag-fps
    • Sadowski I, Stone JC, Pawson T. 1986. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of fujinami sarcoma virus p130gag-fps. Mol. Cell. Biol. 6:4396-408
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4396-4408
    • Sadowski, I.1    Stone, J.C.2    Pawson, T.3
  • 76
    • 0027393849 scopus 로고
    • Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation
    • Shoelson SE, Sivaraja M, Williams KP, Hu P, Schlessinger J, Weiss MA. 1993. Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation. EMBO J. 12:795-802
    • (1993) EMBO J. , vol.12 , pp. 795-802
    • Shoelson, S.E.1    Sivaraja, M.2    Williams, K.P.3    Hu, P.4    Schlessinger, J.5    Weiss, M.A.6
  • 77
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature 385:602-9
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 78
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signalling
    • Songyang Z, Cantley LC. 1995. Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem. Sci. 20:470-75
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 79
    • 0028863102 scopus 로고
    • A single point mutation switches the specificity of group III src homology (SH) 2 domains to that of group I SH2 domains
    • Songyang Z, Gish G, Mbamulu G, Pawson T, Cantley LC. 1995. A single point mutation switches the specificity of group III src homology (SH) 2 domains to that of group I SH2 domains. J. Biol. Chem. 270:26029-32
    • (1995) J. Biol. Chem. , vol.270 , pp. 26029-26032
    • Songyang, Z.1    Gish, G.2    Mbamulu, G.3    Pawson, T.4    Cantley, L.C.5
  • 81
    • 0028351583 scopus 로고
    • Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk and Vav
    • Songyang Z, Shoelson SE, McGlade J, Olivier P, Pawson T, et al. 1994. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk and Vav. Mol. Cell. Biol. 14:2777-85
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2777-2785
    • Songyang, Z.1    Shoelson, S.E.2    McGlade, J.3    Olivier, P.4    Pawson, T.5
  • 83
    • 0029146950 scopus 로고
    • Characterization of a novel protein-binding modular - The WW domain
    • Sudol M, Chen HI, Bougeret C, Bork P. 1995. Characterization of a novel protein-binding modular - the WW domain. FEBS Lett. 369:67-71
    • (1995) FEBS Lett. , vol.369 , pp. 67-71
    • Sudol, M.1    Chen, H.I.2    Bougeret, C.3    Bork, P.4
  • 84
    • 0029278886 scopus 로고
    • Structure-function relationships in Src family and related protein kinases
    • Superti-Furga G, Courtneidge SA. 1995. Structure-function relationships in Src family and related protein kinases. Bioessays 17:321-30
    • (1995) Bioessays , vol.17 , pp. 321-330
    • Superti-Furga, G.1    Courtneidge, S.A.2
  • 85
  • 86
    • 0024435351 scopus 로고
    • Phosphorylation of middle T by pp60c-src: A switch for binding of phosphatidylinositol 3-kinase and optimal tumorigenesis
    • Talmadge DA, Freund R, Young AT, Dahl J, Dawe CJ, Benjamin TL. 1989. Phosphorylation of middle T by pp60c-src: a switch for binding of phosphatidylinositol 3-kinase and optimal tumorigenesis. Cell 59:55-65
    • (1989) Cell , vol.59 , pp. 55-65
    • Talmadge, D.A.1    Freund, R.2    Young, A.T.3    Dahl, J.4    Dawe, C.J.5    Benjamin, T.L.6
  • 87
    • 0028675576 scopus 로고
    • Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos
    • Terasawa H, Kohda D, Hatanaka H, Tsuchiya S, Ogura K, et al. 1994. Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos. Nature Struct. Biol. 1:891-97
    • (1994) Nature Struct. Biol. , vol.1 , pp. 891-897
    • Terasawa, H.1    Kohda, D.2    Hatanaka, H.3    Tsuchiya, S.4    Ogura, K.5
  • 88
    • 0029967679 scopus 로고    scopus 로고
    • Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 Å and 1.8 Å resolution
    • Tong L, Warren TC, King J, Betageri R, Rose J, Jakes S. 1996. Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 Å and 1.8 Å resolution. J. Mol. Biol. 256:601-10
    • (1996) J. Mol. Biol. , vol.256 , pp. 601-610
    • Tong, L.1    Warren, T.C.2    King, J.3    Betageri, R.4    Rose, J.5    Jakes, S.6
  • 89
    • 0029150052 scopus 로고
    • HIV accessory proteins: Leading roles for the supporting cast
    • Trono D. 1995. HIV accessory proteins: leading roles for the supporting cast. Cell 82:189-92
    • (1995) Cell , vol.82 , pp. 189-192
    • Trono, D.1
  • 90
    • 0027506762 scopus 로고
    • Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β subunit and are required for binding of phospholipase Cy and a 64-kilodalton protein, respectively
    • Valius M, Bazenet C, Kazlauskas A. 1993. Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β subunit and are required for binding of phospholipase Cy and a 64-kilodalton protein, respectively. Mol. Cell. Biol. 13:133-43
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 133-143
    • Valius, M.1    Bazenet, C.2    Kazlauskas, A.3
  • 91
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    • Waksman G, Kominos D, Robertson SR, Pant N, Baltimore D, et al. 1992. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358:646-53
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1    Kominos, D.2    Robertson, S.R.3    Pant, N.4    Baltimore, D.5
  • 92
    • 0027409064 scopus 로고
    • Binding of a high affinity phophotyrosyl peptide to the src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J. 1993. Binding of a high affinity phophotyrosyl peptide to the src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72:779-90
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 93
    • 0027328526 scopus 로고
    • Tandem SH2 domains of ZAP-70 bind to T-cell antigen receptor zeta and CD3 epsilon
    • Wange RL, Malek SN, Desiderio S, Samelson LE. 1993. Tandem SH2 domains of ZAP-70 bind to T-cell antigen receptor zeta and CD3 epsilon J. Biol. Chem. 268:19797-801
    • (1993) J. Biol. Chem. , vol.268 , pp. 19797-19801
    • Wange, R.L.1    Malek, S.N.2    Desiderio, S.3    Samelson, L.E.4
  • 94
    • 0027315182 scopus 로고
    • T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases
    • Weiss A. 1993. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73:209-12
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 95
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman M, Kaplan DR, Schaffhausen B, Cantley L, Roberts TM. 1985. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315:239-42
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4    Roberts, T.M.5
  • 96
    • 0029643950 scopus 로고
    • Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk
    • Wu X, Knudsen B, Feller SM, Zheng J, Sali A, et al. 1995. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 3:215-26
    • (1995) Structure , vol.3 , pp. 215-226
    • Wu, X.1    Knudsen, B.2    Feller, S.M.3    Zheng, J.4    Sali, A.5
  • 98
    • 0028906357 scopus 로고
    • Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide
    • Xu RX, Word JM, Davis DG, Rink MJ, Willard DH Jr., Gampe RT Jr. 1995. Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide. Biochemistry 34:2107-21
    • (1995) Biochemistry , vol.34 , pp. 2107-2121
    • Xu, R.X.1    Word, J.M.2    Davis, D.G.3    Rink, M.J.4    Willard Jr., D.H.5    Gampe Jr., R.T.6
  • 99
  • 100
    • 0027102571 scopus 로고
    • Solution structure of the SH3 domain of Src and identification of its ligand-binding site
    • Yu H, Rosen MK, Shin TB, Seidel-Duggan C, Brugge JS, Schreiber SL. 1992. Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science 258:1665-68
    • (1992) Science , vol.258 , pp. 1665-1668
    • Yu, H.1    Rosen, M.K.2    Shin, T.B.3    Seidel-Duggan, C.4    Brugge, J.S.5    Schreiber, S.L.6
  • 102
    • 0029121483 scopus 로고
    • Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor
    • Zhou MM, Meadows RP, Logan TM, Yoon HS, Wade WS, et al. 1995. Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proc. Natl. Acad. Sci. USA 92:7784-88
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7784-7788
    • Zhou, M.M.1    Meadows, R.P.2    Logan, T.M.3    Yoon, H.S.4    Wade, W.S.5
  • 103


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