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Volumn 5, Issue 10, 1997, Pages 1361-1372

The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling

Author keywords

Crystal structure; Fyn protein tyrosine kinase; HIV 1; Nef protein; SH3 domain

Indexed keywords


EID: 0031572847     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00286-4     Document Type: Article
Times cited : (191)

References (73)
  • 1
    • 0022382732 scopus 로고
    • A new HTLV-III/LAV encoded antigen detected by antibodies from AIDS patients
    • Allan, J.S., et al., & Essex, M. (1985). A new HTLV-III/LAV encoded antigen detected by antibodies from AIDS patients. Science 230, 810-813.
    • (1985) Science , vol.230 , pp. 810-813
    • Allan, J.S.1    Essex, M.2
  • 2
    • 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, 189-192.
    • (1995) Cell , vol.82 , pp. 189-192
    • Trono, D.1
  • 3
    • 0028466226 scopus 로고
    • Immunodeficiency viruses. Not enough sans Nef
    • Littman, D.R. (1994). Immunodeficiency viruses. Not enough sans Nef. Curr. Biol. 4, 618-620.
    • (1994) Curr. Biol. , vol.4 , pp. 618-620
    • Littman, D.R.1
  • 4
    • 0028173343 scopus 로고
    • The role of Nef in the replication cycle of the human and simian immunodeficiency viruses
    • Cullen, B.R. (1994). The role of Nef in the replication cycle of the human and simian immunodeficiency viruses. Virology 205, 1-6.
    • (1994) Virology , vol.205 , pp. 1-6
    • Cullen, B.R.1
  • 5
    • 0025743306 scopus 로고
    • Importance of the nef gene for maintenance of high virus loads and for development of AIDS
    • Kestler, H.W., et al., & Desrosiers, R.C. (1991). Importance of the nef gene for maintenance of high virus loads and for development of AIDS. Cell 65, 651-662.
    • (1991) Cell , vol.65 , pp. 651-662
    • Kestler, H.W.1    Desrosiers, R.C.2
  • 6
    • 0029089406 scopus 로고
    • Identification of a nef allele that causes lymphocyte activation and acute disease in macaque monkeys
    • Du, Z., et al., & Desrosiers, R.C. (1995). Identification of a nef allele that causes lymphocyte activation and acute disease in macaque monkeys. Cell 82, 665-674.
    • (1995) Cell , vol.82 , pp. 665-674
    • Du, Z.1    Desrosiers, R.C.2
  • 7
    • 0028944667 scopus 로고
    • Pathogenicity of live attenuated SIV after mucosal infection of neonatal macaques
    • Baba, T.W., et al., & Ruprecht, R.M. (1995). Pathogenicity of live attenuated SIV after mucosal infection of neonatal macaques. Science 267, 1820-1825.
    • (1995) Science , vol.267 , pp. 1820-1825
    • Baba, T.W.1    Ruprecht, R.M.2
  • 8
    • 0027043276 scopus 로고
    • Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene
    • Daniel, M.D., Kirchhoff, F., Czajak, S.C., Sehgal, P.K. & Desrosiers, R.C. (1992). Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene. Science 258, 1938-1941.
    • (1992) Science , vol.258 , pp. 1938-1941
    • Daniel, M.D.1    Kirchhoff, F.2    Czajak, S.C.3    Sehgal, P.K.4    Desrosiers, R.C.5
  • 9
    • 0028835788 scopus 로고
    • Brief report: Absence of intact nef sequences in a long-term survivor with nonprogressive HIV-1 infection
    • Kirchhoff, F., Greenough, T.C., Brettler, D.B., Sullivan, J.L. & Desrosiers, R.C. (1995). Brief report: absence of intact nef sequences in a long-term survivor with nonprogressive HIV-1 infection. N. Engl. J. Med. 332, 228-232.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 228-232
    • Kirchhoff, F.1    Greenough, T.C.2    Brettler, D.B.3    Sullivan, J.L.4    Desrosiers, R.C.5
  • 10
    • 0028804160 scopus 로고
    • Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients
    • Deacon, N.J., et al., & Mills, J. (1995). Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients. Science 270, 988-991.
    • (1995) Science , vol.270 , pp. 988-991
    • Deacon, N.J.1    Mills, J.2
  • 11
    • 0023659754 scopus 로고
    • HIV F/3• orf encodes a phosphorylated GTP-binding protein resembling an oncogene product
    • Guy, B., et al., & Lecocq, J.P. (1987). HIV F/3• orf encodes a phosphorylated GTP-binding protein resembling an oncogene product. Nature 330, 266-269.
    • (1987) Nature , vol.330 , pp. 266-269
    • Guy, B.1    Lecocq, J.P.2
  • 12
    • 0030014162 scopus 로고    scopus 로고
    • Producer-cell modification of human immunodeficiency virus type 1 : Nef is a virion protein
    • Pandori, M.W., et al., & Guatelli, J.C. (1996). Producer-cell modification of human immunodeficiency virus type 1 : Nef is a virion protein. J. Virol. 70, 4283-4290.
    • (1996) J. Virol. , vol.70 , pp. 4283-4290
    • Pandori, M.W.1    Guatelli, J.C.2
  • 13
    • 0029975546 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef protein is incorporated into virus particles and specifically cleaved by the viral proteinase
    • Welker, R., Kottler, H., Kalbitzer, H.R. & Krausslich, H.G. (1996). Human immunodeficiency virus type 1 Nef protein is incorporated into virus particles and specifically cleaved by the viral proteinase. Virology 219, 228-236.
    • (1996) Virology , vol.219 , pp. 228-236
    • Welker, R.1    Kottler, H.2    Kalbitzer, H.R.3    Krausslich, H.G.4
  • 14
    • 0029970825 scopus 로고    scopus 로고
    • Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases
    • Schorr, J., et al., & Kalbitzer, H.R. (1996). Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases. J. Virol. 70, 9051-9054.
    • (1996) J. Virol. , vol.70 , pp. 9051-9054
    • Schorr, J.1    Kalbitzer, H.R.2
  • 15
    • 0027999147 scopus 로고
    • A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease
    • Freund, J., et al., & Kalbitzer, H.R. (1 994). A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease. Eur. J. Biochem. 223, 589-593.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 589-593
    • Freund, J.1    Kalbitzer, H.R.2
  • 16
    • 0028180868 scopus 로고
    • Nef induces CD4 endocytosis: Requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain
    • Aiken, C., Konner, J., Landau, N.R., Lenburg, M.E. & Trono, D. (1994). Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain. Cell 76, 853-864.
    • (1994) Cell , vol.76 , pp. 853-864
    • Aiken, C.1    Konner, J.2    Landau, N.R.3    Lenburg, M.E.4    Trono, D.5
  • 17
    • 0028843339 scopus 로고
    • Human immunodeficiency virus type 1 Nef and p56lck protein-tyrosine kinase interact with a common element in CD4 cytoplasmic tail
    • Salghetti, S., Mariani, R. & Skowronski, J. (1995). Human immunodeficiency virus type 1 Nef and p56lck protein-tyrosine kinase interact with a common element in CD4 cytoplasmic tail. Proc. Natl. Acad. Sci. USA 92, 349-353.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 349-353
    • Salghetti, S.1    Mariani, R.2    Skowronski, J.3
  • 18
    • 0028924785 scopus 로고
    • Human immunodeficiency virus type 1 Nef induces accumulation of CD4 in early endosomes
    • Schwartz, O., et al., & Danos, O. (1995). Human immunodeficiency virus type 1 Nef induces accumulation of CD4 in early endosomes. J. Virol. 69, 528-533.
    • (1995) J. Virol. , vol.69 , pp. 528-533
    • Schwartz, O.1    Danos, O.2
  • 19
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein
    • Schwartz, O., Marechal, V., Le Gall, S., Lemonnier, F. & Heard, J.M. (1996). Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat. Med. 2, 338-342.
    • (1996) Nat. Med. , vol.2 , pp. 338-342
    • Schwartz, O.1    Marechal, V.2    Le Gall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 20
    • 0031039979 scopus 로고    scopus 로고
    • Separable functions of Nef disrupt two aspects of T cell receptor machinery: CD4 expression and CD3 signaling
    • Iafrate, A.J., Bronson, S. & Skowronski, J. (1997). Separable functions of Nef disrupt two aspects of T cell receptor machinery: CD4 expression and CD3 signaling. EMBO J. 16, 673-684.
    • (1997) EMBO J. , vol.16 , pp. 673-684
    • Iafrate, A.J.1    Bronson, S.2    Skowronski, J.3
  • 21
    • 0028887886 scopus 로고
    • Human immunodeficiency virus type 1 Nef protein inhibits activation pathways in peripheral blood mononuclear cells and T-cell lines
    • Greenway, A., Azad, A. & McPhee, D. (1995). Human immunodeficiency virus type 1 Nef protein inhibits activation pathways in peripheral blood mononuclear cells and T-cell lines. J. Virol. 69, 1842-1850.
    • (1995) J. Virol. , vol.69 , pp. 1842-1850
    • Greenway, A.1    Azad, A.2    McPhee, D.3
  • 22
    • 0027533215 scopus 로고
    • Altered T cell activation and development in transgenic mice expressing the HIV-1 nef gene
    • Skowronski, J., Parks, D. & Mariani, R. (1 993). Altered T cell activation and development in transgenic mice expressing the HIV-1 nef gene. EMBO J. 12, 703-713.
    • (1993) EMBO J. , vol.12 , pp. 703-713
    • Skowronski, J.1    Parks, D.2    Mariani, R.3
  • 23
    • 0028302998 scopus 로고
    • Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene
    • Chowers, M.Y., et al., & Guatelli, J.C. (1994). Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene. J. Virol. 68, 2906-2914.
    • (1994) J. Virol. , vol.68 , pp. 2906-2914
    • Chowers, M.Y.1    Guatelli, J.C.2
  • 24
    • 0027956402 scopus 로고
    • The HIV-1 nef gene acts as a positive viral infectivity factor
    • Miller, M.D., Feinberg, M.B. & Greene, W.C. (1994). The HIV-1 nef gene acts as a positive viral infectivity factor. Trends Microbiol. 2, 294-298.
    • (1994) Trends Microbiol. , vol.2 , pp. 294-298
    • Miller, M.D.1    Feinberg, M.B.2    Greene, W.C.3
  • 25
    • 0029015330 scopus 로고
    • Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis
    • Aiken, C. & Trono, D. (1995). Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis. J. Virol. 69, 5048-5056.
    • (1995) J. Virol. , vol.69 , pp. 5048-5056
    • Aiken, C.1    Trono, D.2
  • 27
    • 0028820530 scopus 로고
    • The growth advantage conferred by HIV-1 nef is determined at the level of viral DNA formation and is independent of CD4 downregulation
    • Chowers, M.Y., Pandori, M.W., Spina, C.A., Richman, D.D. & Guatelli, J.C. (1995). The growth advantage conferred by HIV-1 nef is determined at the level of viral DNA formation and is independent of CD4 downregulation. Virology 212, 451-457.
    • (1995) Virology , vol.212 , pp. 451-457
    • Chowers, M.Y.1    Pandori, M.W.2    Spina, C.A.3    Richman, D.D.4    Guatelli, J.C.5
  • 28
    • 0029835631 scopus 로고    scopus 로고
    • The association of Nef with a cellular serine/threonine kinase and its enhancement of infectivity are viral isolate dependent
    • Luo, T. & Garcia, J.V. (1996). The association of Nef with a cellular serine/threonine kinase and its enhancement of infectivity are viral isolate dependent. J. Virol. 70, 6493-6496.
    • (1996) J. Virol. , vol.70 , pp. 6493-6496
    • Luo, T.1    Garcia, J.V.2
  • 29
    • 0027958148 scopus 로고
    • Human immunodeficiency virus type 1 Nef associates with a cellular serine kinase in T lymphocytes
    • Sawai, E.T., et al., & Cheng-Mayer, C. (1994). Human immunodeficiency virus type 1 Nef associates with a cellular serine kinase in T lymphocytes. Proc. Natl. Acad. Sci. USA 91, 1539-1543.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1539-1543
    • Sawai, E.T.1    Cheng-Mayer, C.2
  • 30
    • 0029793714 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef associates with a member of the p21 -activated kinase family
    • Nunn, M.F. & Marsh, J.W. (1996). Human immunodeficiency virus type 1 Nef associates with a member of the p21 -activated kinase family. J. Virol. 70, 6157-6161.
    • (1996) J. Virol. , vol.70 , pp. 6157-6161
    • Nunn, M.F.1    Marsh, J.W.2
  • 31
    • 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., et al., & Saksella, K. (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, 5006-5015.
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.H.1    Saksella, K.2
  • 32
    • 0029962938 scopus 로고    scopus 로고
    • Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects
    • Collette, Y., et al., & Olive, D. (1996). Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects. J. Biol. Chem. 271, 6333-6341.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6333-6341
    • Collette, Y.1    Olive, D.2
  • 33
    • 0029819124 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef binds directly to Lck and mitogen-activated protein kinase, inhibiting kinase activity
    • Greenway, A., Azad, A., Mills, J. & McPhee, D. (1996). Human immunodeficiency virus type 1 Nef binds directly to Lck and mitogen-activated protein kinase, inhibiting kinase activity. J. Virol. 70, 6701-6708.
    • (1996) J. Virol. , vol.70 , pp. 6701-6708
    • Greenway, A.1    Azad, A.2    Mills, J.3    McPhee, D.4
  • 34
    • 0028958025 scopus 로고
    • Src family protein tyrosine kinases and cellular signal transduction pathways
    • Erpel, T. & Courtneidge, S.A. (1995). Src family protein tyrosine kinases and cellular signal transduction pathways. Curr. Opin. Cell Biol. 7, 176-182.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 176-182
    • Erpel, T.1    Courtneidge, S.A.2
  • 35
    • 0028926070 scopus 로고
    • Transmembrane signaling by antigen receptors of B and T lymphocytes
    • DeFranco, A.L. (1995). Transmembrane signaling by antigen receptors of B and T lymphocytes. Curr. Opin. Cell Biol. 7, 163-175.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 163-175
    • DeFranco, A.L.1
  • 36
    • 0028887998 scopus 로고
    • Multiple kinases mediate T-cell-receptor signaling
    • Howe, L.R. & Weiss, A. (1995). Multiple kinases mediate T-cell-receptor signaling. Trends Biochem. Sci. 20, 59-64.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 59-64
    • Howe, L.R.1    Weiss, A.2
  • 37
    • 0030061514 scopus 로고    scopus 로고
    • Catalytic activity of the mouse guanine nucleotide exchanger mSOS is activated by Fyn tyrosine kinase and the T-cell antigen receptor in T cells
    • Li, B., et al., & Kamata, B. (1996). Catalytic activity of the mouse guanine nucleotide exchanger mSOS is activated by Fyn tyrosine kinase and the T-cell antigen receptor in T cells. Proc. Natl. Acad. Sci. USA 93, 1001-1005.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1001-1005
    • Li, B.1    Kamata, B.2
  • 38
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., Irving, B.A., van Oers, N.S., Chan, A.C. & Weiss, A. (1994). Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263, 1136-1139.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.3    Chan, A.C.4    Weiss, A.5
  • 39
    • 0026667341 scopus 로고
    • Activation of tyrosine kinase p60fyn following T cell antigen receptor cross-linking
    • Tsygankov, A.Y., Broker, B.M., Fargnoli, J., Ledbetter, J.A. & Bolen, J.B. (1992). Activation of tyrosine kinase p60fyn following T cell antigen receptor cross-linking. J. Biol. Chem. 267, 18259-18262.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18259-18262
    • Tsygankov, A.Y.1    Broker, B.M.2    Fargnoli, J.3    Ledbetter, J.A.4    Bolen, J.B.5
  • 40
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. (1995). Protein modules and signaling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 41
    • 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, U.A., Chait, B.T. & Kuriyan, J. (1996). Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85, 931-942.
    • (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
  • 42
    • 0023506572 scopus 로고
    • Isolation and sequence of a cDNA corresponding to a src-related gene expressed in murine hemopoietic cells
    • Holtzman, D.A., Cook, W.D. & Dunn, A.R. (1987). Isolation and sequence of a cDNA corresponding to a src-related gene expressed in murine hemopoietic cells. Proc. Natl. Acad. Sci. USA 84, 8325-8329.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8325-8329
    • Holtzman, D.A.1    Cook, W.D.2    Dunn, A.R.3
  • 43
    • 0027080147 scopus 로고
    • The Src family of tyrosine protein kinases in hemopoietic signal transduction
    • Bolen, J.B., Rowley, R.B., Spana, C. & Tsygankov, A.Y. (1992). The Src family of tyrosine protein kinases in hemopoietic signal transduction. FASEB J. 6, 3403-3409.
    • (1992) FASEB J. , vol.6 , pp. 3403-3409
    • Bolen, J.B.1    Rowley, R.B.2    Spana, C.3    Tsygankov, A.Y.4
  • 44
    • 0028258948 scopus 로고
    • Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1
    • Freund, J., et al., & Kalbitzer, H.R. (1994). Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1. Eur. J. Biochem. 221, 811-819.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 811-819
    • Freund, J.1    Kalbitzer, H.R.2
  • 45
    • 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., et al., & Wingfield, P.T. (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. Nat. Struct. Biol. 3, 340-345.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Wingfield, P.T.2
  • 46
    • 0030980288 scopus 로고    scopus 로고
    • Refined solution structure and backbone dynamics of HIV-1 Nef
    • Grzesiek, S., et al., & Wingfield, PT. (1997). Refined solution structure and backbone dynamics of HIV-1 Nef. Protein Sci. 6, 1248-1263.
    • (1997) Protein Sci. , vol.6 , pp. 1248-1263
    • Grzesiek, S.1    Wingfield, P.T.2
  • 47
    • 0027245080 scopus 로고
    • Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin
    • Noble, E.M., Musacchio, A., Saraste, M., Courtneidge, S.A. & Wierenge, R.K. (1993). Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12, 2617-2624.
    • (1993) EMBO J. , vol.12 , pp. 2617-2624
    • Noble, E.M.1    Musacchio, A.2    Saraste, M.3    Courtneidge, S.A.4    Wierenge, R.K.5
  • 48
    • 0030597148 scopus 로고    scopus 로고
    • Clustered localization of oligomeric Nef protein of human immunodeficiency virus type 1 on the cell surface
    • Fujii, Y., et al., & Adachi, A. (1996). Clustered localization of oligomeric Nef protein of human immunodeficiency virus type 1 on the cell surface. FEBS Lett. 395, 257-261.
    • (1996) FEBS Lett. , vol.395 , pp. 257-261
    • Fujii, Y.1    Adachi, A.2
  • 49
    • 0027273325 scopus 로고
    • Oligomerization of the Nef protein from human immunodeficiency virus (HIV) type 1
    • Kienzle, N., Freund, J., Kalbitzer, H.R. & Mueller-Lantzsch, N. (1993). Oligomerization of the Nef protein from human immunodeficiency virus (HIV) type 1. Eur. J. Biochem. 214, 451-457.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 451-457
    • Kienzle, N.1    Freund, J.2    Kalbitzer, H.R.3    Mueller-Lantzsch, N.4
  • 50
    • 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. Nat. Struct. Biol. 1, 546-551.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 51
    • 0029753011 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of Pl3-kinase
    • Renzoni, D.A., et al., & Ladbury, J.E. (1996). Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of Pl3-kinase. Biochemistry 35, 15646-15653.
    • (1996) Biochemistry , vol.35 , pp. 15646-15653
    • Renzoni, D.A.1    Ladbury, J.E.2
  • 52
    • 0030585430 scopus 로고    scopus 로고
    • Solution structure and peptide binding of the SH3 domain from human Fyn
    • Morton, C.J., et al., & Campbell, I.D. (1996). Solution structure and peptide binding of the SH3 domain from human Fyn. Structure 4, 705-714.
    • (1996) Structure , vol.4 , pp. 705-714
    • Morton, C.J.1    Campbell, I.D.2
  • 53
    • 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., et al., & Kuriyan, J. (1995). Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 3, 215-226,
    • (1995) Structure , vol.3 , pp. 215-226
    • Wu, X.1    Kuriyan, J.2
  • 54
    • 0029157039 scopus 로고
    • Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions
    • Weng, Z., et al., & Brugge, J.S. (1995). Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions. Mol. Cell Biol. 15, 5627-5634.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 5627-5634
    • Weng, Z.1    Brugge, J.S.2
  • 55
    • 0027259393 scopus 로고
    • Analysis of human immunodeficiency virus type 1 nef gene sequences present in vivo
    • Shugars, D.C., et al., & Swanstrom, R. (1993). Analysis of human immunodeficiency virus type 1 nef gene sequences present in vivo. J. Virol. 67, 4639-4650.
    • (1993) J. Virol. , vol.67 , pp. 4639-4650
    • Shugars, D.C.1    Swanstrom, R.2
  • 56
    • 0030246983 scopus 로고    scopus 로고
    • Sequence heterogeneity of Nef transcripts in HIV-1-infected subjects at different stages of disease
    • Ratner, L., et al., & Arens, M. (1996). Sequence heterogeneity of Nef transcripts in HIV-1-infected subjects at different stages of disease. Virology 223, 245-250.
    • (1996) Virology , vol.223 , pp. 245-250
    • Ratner, L.1    Arens, M.2
  • 57
    • 0029586759 scopus 로고
    • Protein-protein interaction at crystal contacts
    • Janin, J. & Rodier, F. (1995). Protein-protein interaction at crystal contacts. Proteins 23, 580-587.
    • (1995) Proteins , vol.23 , pp. 580-587
    • Janin, J.1    Rodier, F.2
  • 58
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., Gorina, S., Jeffrey, P. & Pavletich, N.P. (1994). Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265, 346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.3    Pavletich, N.P.4
  • 59
    • 0030056871 scopus 로고    scopus 로고
    • Physical and functional interactions of protein tyrosine kinases, p59fyn and ZAP-70, in T cell signaling
    • Fusaki, N., Matsuda, S., Nishizumi, H., Umemori, H. & Yamamoto, T. (1996). Physical and functional interactions of protein tyrosine kinases, p59fyn and ZAP-70, in T cell signaling. J. Immunol. 156, 1369-1377.
    • (1996) J. Immunol. , vol.156 , pp. 1369-1377
    • Fusaki, N.1    Matsuda, S.2    Nishizumi, H.3    Umemori, H.4    Yamamoto, T.5
  • 60
    • 0029910821 scopus 로고    scopus 로고
    • CD43-specific activation of T cells induces association of CD43 to Fyn kinase
    • Pedrava-Alva, G., Mérida, L.B., Burakoff, S.J. & Rosenstein, Y. (1996). CD43-specific activation of T cells induces association of CD43 to Fyn kinase. J. Biol. Chem. 271, 27564-27568.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27564-27568
    • Pedrava-Alva, G.1    Mérida, L.B.2    Burakoff, S.J.3    Rosenstein, Y.4
  • 61
    • 0029868036 scopus 로고    scopus 로고
    • A physical interaction between the cell death protein Fas and tyrosine kinase p59
    • Atkinson, E.A., et al., & Bleackley, R.C. (1 996). A physical interaction between the cell death protein Fas and tyrosine kinase p59. J. Biol. Chem. 271, 5968-5971.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5968-5971
    • Atkinson, E.A.1    Bleackley, R.C.2
  • 62
    • 0030902281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling
    • Qian, D., et al., & Weiss, A. (1997). Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling. J. Exp. Med. 185, 1253-1259.
    • (1997) J. Exp. Med. , vol.185 , pp. 1253-1259
    • Qian, D.1    Weiss, A.2
  • 63
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi, I., et al., & Miller, W.T. (1997). Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653.
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1    Miller, W.T.2
  • 64
    • 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, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 65
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993). Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 66
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project, No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 67
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 69
    • 0001185158 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. (1993). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. D 49, 148-157.
    • (1993) Acta Cryst. D , vol.49 , pp. 148-157
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 70
    • 0001513485 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R., MacArthur, M., Moss, D. & Thornton, J. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 91-97.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 91-97
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 71
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 72
    • 0028057108 scopus 로고
    • Raster 3D version 2.0 - A program for photorealistic molecular graphics
    • Meritt, E.A. & Murphy, M.E.P. (1994). Raster 3D version 2.0 - a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Meritt, E.A.1    Murphy, M.E.P.2
  • 73
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.