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Volumn 8, Issue 9, 2013, Pages

High Resolution Crystal Structure of the Grb2 SH2 Domain with a Phosphopeptide Derived from CD28

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; PHOSPHOPEPTIDE; PROLINE; PROTEIN SH2;

EID: 84884753653     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0074482     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, Lammers R, et al. (1992) The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 70: 431-442.
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3    Li, W.4    Margolis, B.5    Lammers, R.6
  • 2
    • 0026678172 scopus 로고
    • Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock M, McGlade J, Mbamalu G, Pelicci G, Daly R, et al. (1992) Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 360: 689-692.
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1    McGlade, J.2    Mbamalu, G.3    Pelicci, G.4    Daly, R.5
  • 3
    • 0030849715 scopus 로고    scopus 로고
    • Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2
    • McNemar C, Snow ME, Windsor WT, Prongay A, Mui P, et al. (1997) Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2. Biochemistry 36: 10006-10014.
    • (1997) Biochemistry , vol.36 , pp. 10006-10014
    • McNemar, C.1    Snow, M.E.2    Windsor, W.T.3    Prongay, A.4    Mui, P.5
  • 4
    • 0033546119 scopus 로고    scopus 로고
    • Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide
    • Ogura K, Tsuchiya S, Terasawa H, Yuzawa S, Hatanaka H, et al. (1999) Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide. J Mol Biol 289: 439-445.
    • (1999) J Mol Biol , vol.289 , pp. 439-445
    • Ogura, K.1    Tsuchiya, S.2    Terasawa, H.3    Yuzawa, S.4    Hatanaka, H.5
  • 5
    • 15844398102 scopus 로고    scopus 로고
    • Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode
    • Rahuel J, Gay B, Erdmann D, Strauss A, Garcia-Echeverria C, et al. (1996) Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode. Nat Struct Biol 3: 586-589.
    • (1996) Nat Struct Biol , vol.3 , pp. 586-589
    • Rahuel, J.1    Gay, B.2    Erdmann, D.3    Strauss, A.4    Garcia-Echeverria, C.5
  • 6
    • 0029811093 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain
    • Thornton KH, Mueller WT, McConnell P, Zhu G, Saltiel AR, et al. (1996) Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain. Biochemistry 35: 11852-11864.
    • (1996) Biochemistry , vol.35 , pp. 11852-11864
    • Thornton, K.H.1    Mueller, W.T.2    McConnell, P.3    Zhu, G.4    Saltiel, A.R.5
  • 7
    • 0036304080 scopus 로고    scopus 로고
    • Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor
    • Nioche P, Liu WQ, Broutin I, Charbonnier F, Latreille MT, et al. (2002) Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor. J Mol Biol 315: 1167-1177.
    • (2002) J Mol Biol , vol.315 , pp. 1167-1177
    • Nioche, P.1    Liu, W.Q.2    Broutin, I.3    Charbonnier, F.4    Latreille, M.T.5
  • 8
    • 0024327899 scopus 로고
    • Clonal expansion versus functional clonal inactivation: a costimulatory signalling pathway determines the outcome of T cell antigen receptor occupancy
    • Mueller DL, Jenkins MK, Schwartz RH, (1989) Clonal expansion versus functional clonal inactivation: a costimulatory signalling pathway determines the outcome of T cell antigen receptor occupancy. Annu Rev Immunol 7: 445-480.
    • (1989) Annu Rev Immunol , vol.7 , pp. 445-480
    • Mueller, D.L.1    Jenkins, M.K.2    Schwartz, R.H.3
  • 9
  • 10
    • 0142259712 scopus 로고    scopus 로고
    • Unifying concepts in CD28, ICOS and CTLA4 co-receptor signalling
    • Rudd CE, Schneider H, (2003) Unifying concepts in CD28, ICOS and CTLA4 co-receptor signalling. Nat Rev Immunol 3: 544-556.
    • (2003) Nat Rev Immunol , vol.3 , pp. 544-556
    • Rudd, C.E.1    Schneider, H.2
  • 11
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, Lilie H, (1996) In vitro folding of inclusion body proteins. FASEB J 10: 49-56.
    • (1996) FASEB J , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 14
    • 34250867814 scopus 로고    scopus 로고
    • Ligand preorganization may be accompanied by entropic penalties in protein-ligand interactions
    • Benfield AP, Teresk MG, Plake HR, DeLorbe JE, Millspaugh LE, et al. (2006) Ligand preorganization may be accompanied by entropic penalties in protein-ligand interactions. Angew Chem Int Ed Engl 118: 6984-6989.
    • (2006) Angew Chem Int Ed Engl , vol.118 , pp. 6984-6989
    • Benfield, A.P.1    Teresk, M.G.2    Plake, H.R.3    DeLorbe, J.E.4    Millspaugh, L.E.5
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ, (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24: 946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 78649233754 scopus 로고    scopus 로고
    • Thermodynamic and structural effects of macrocyclic constraints in protein-ligand interactions
    • DeLorbe JE, Clements JH, Whiddon BB, Martin SF, (2010) Thermodynamic and structural effects of macrocyclic constraints in protein-ligand interactions. ACS Med Chem Lett 1: 448-452.
    • (2010) ACS Med Chem Lett , vol.1 , pp. 448-452
    • DeLorbe, J.E.1    Clements, J.H.2    Whiddon, B.B.3    Martin, S.F.4
  • 19
    • 0033602525 scopus 로고    scopus 로고
    • Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2
    • Ettmayer P, France D, Gounarides J, Jarosinski M, Martin MS, et al. (1999) Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2. J Med Chem 42: 971-980.
    • (1999) J Med Chem , vol.42 , pp. 971-980
    • Ettmayer, P.1    France, D.2    Gounarides, J.3    Jarosinski, M.4    Martin, M.S.5
  • 20
    • 81355127252 scopus 로고    scopus 로고
    • Functional implications of the conformational switch in AICD peptide upon binding to Grb2-SH2 domain
    • Das S, Raychaudhuri M, Sen U, Mukhopadhyay D, (2011) Functional implications of the conformational switch in AICD peptide upon binding to Grb2-SH2 domain. J Mol Biol 414: 217-230.
    • (2011) J Mol Biol , vol.414 , pp. 217-230
    • Das, S.1    Raychaudhuri, M.2    Sen, U.3    Mukhopadhyay, D.4
  • 22
    • 0032546729 scopus 로고    scopus 로고
    • Structural basis for the high affinity of amino-aromatic SH2 phosphopeptide ligands
    • Rahuel J, Garcia-Echeverria C, Furet P, Strauss A, Caravatti G, et al. (1998) Structural basis for the high affinity of amino-aromatic SH2 phosphopeptide ligands. J Mol Biol 279: 1013-1022.
    • (1998) J Mol Biol , vol.279 , pp. 1013-1022
    • Rahuel, J.1    Garcia-Echeverria, C.2    Furet, P.3    Strauss, A.4    Caravatti, G.5
  • 23
    • 0029878266 scopus 로고    scopus 로고
    • Crystal structure of the PI3-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 PI3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nat Struct Biol 3: 364-374.
    • (1996) Nat Struct Biol , vol.3 , pp. 364-374
    • Nolte, R.T.1    Eck, M.J.2    Schlessinger, J.3    Shoelson, S.E.4    Harrison, S.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.