메뉴 건너뛰기




Volumn 5, Issue 6, 2010, Pages

Conformational determinants of phosphotyrosine peptides complexed with the Src SH2 domain

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; ISOLEUCINE; LIGAND; PHOSPHOPEPTIDE; PHOSPHOTYROSINE; POLYPEPTIDE; PEPTIDE;

EID: 77955295230     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011215     Document Type: Article
Times cited : (11)

References (34)
  • 2
    • 0026023289 scopus 로고
    • Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
    • Soriano P, Montgomery C, Geske R, Bradley A (1991) Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64: 693-702.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 3
    • 0026612467 scopus 로고
    • Requirement ofpp60c-src expression for osteoclasts to form ruffled borders and resorb bone inmice
    • Boyce BF, Yoneda T, Lowe C, Soriano P, Mundy GR (1992) Requirement ofpp60c-src expression for osteoclasts to form ruffled borders and resorb bone inmice. J Clin Invest 90: 1622-1627.
    • (1992) J Clin Invest , vol.90 , pp. 1622-1627
    • Boyce, B.F.1    Yoneda, T.2    Lowe, C.3    Soriano, P.4    Mundy, G.R.5
  • 4
    • 0028898383 scopus 로고
    • Sequencerequirements for binding of Src family tyrosine kinases to activated growthfactor receptors
    • Alonso G, Koegl M, Mazurenko N, Courtneidge SA (1995) Sequencerequirements for binding of Src family tyrosine kinases to activated growthfactor receptors. J Biol Chem 270: 9840-9848.
    • (1995) J Biol Chem , vol.270 , pp. 9840-9848
    • Alonso, G.1    Koegl, M.2    Mazurenko, N.3    Courtneidge, S.A.4
  • 5
  • 6
    • 0027409064 scopus 로고
    • Binding of ahigh affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures ofthe complexed and peptide-free forms
    • Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J (1993) Binding of ahigh affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures ofthe complexed and peptide-free forms. Cell 72: 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 7
    • 0028130221 scopus 로고
    • Peptideinhibitors of src SH3-SH2-phosphoprotein interactions
    • Gilmer T, Rodriguez M, Jordan S, Crosby R, Alligood K, et al. (1994) Peptideinhibitors of src SH3-SH2-phosphoprotein interactions. J Biol Chem 269:31711-31719.
    • (1994) J Biol Chem , vol.269 , pp. 31711-31719
    • Gilmer, T.1    Rodriguez, M.2    Jordan, S.3    Crosby, R.4    Alligood, K.5
  • 8
    • 0028906357 scopus 로고
    • Solutionstructure of the human pp60c-src SH2 domain complexed with a phosphorylatedtyrosine pentapeptide
    • Xu RX, Word JM, Davis DG, Rink MJ, Willard DH, Jr., et al. (1995) Solutionstructure of the human pp60c-src SH2 domain complexed with a phosphorylatedtyrosine pentapeptide. Biochemistry 34: 2107-2121.
    • (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
  • 9
    • 0032560622 scopus 로고    scopus 로고
    • Probing the "twoprongedplug two-holed socket" model for the mechanism of binding of the SrcSH2 domain to phosphotyrosyl peptides: A thermodynamic study
    • Bradshaw JM, Grucza RA, Ladbury JE, Waksman G (1998) Probing the "twoprongedplug two-holed socket" model for the mechanism of binding of the SrcSH2 domain to phosphotyrosyl peptides: a thermodynamic study. Biochemistry37: 9083-9090.
    • (1998) Biochemistry37 , pp. 9083-9090
    • Bradshaw, J.M.1    Grucza, R.A.2    Ladbury, J.E.3    Waksman, G.4
  • 10
    • 0037116524 scopus 로고    scopus 로고
    • Calorimetricand structural studies of 1,2,3-trisubstituted cyclopropanes as conformationallyconstrained peptide inhibitors of Src SH2 domain binding
    • Davidson JP, Lubman O, Rose T, Waksman G, Martin SF (2002) Calorimetricand structural studies of 1,2,3-trisubstituted cyclopropanes as conformationallyconstrained peptide inhibitors of Src SH2 domain binding. J Am Chem Soc 124:205-215.
    • (2002) J Am Chem Soc , vol.124 , pp. 205-215
    • Davidson, J.P.1    Lubman, O.2    Rose, T.3    Waksman, G.4    Martin, S.F.5
  • 11
    • 2542528563 scopus 로고    scopus 로고
    • Conformationally constrained peptideanalogues of pTyr-Glu-Glu-Ile as inhibitors of the Src SH2 domain binding
    • Nam NH, Ye G, Sun G, Parang K (2004) Conformationally constrained peptideanalogues of pTyr-Glu-Glu-Ile as inhibitors of the Src SH2 domain binding.J Med Chem 47: 3131-3141.
    • (2004) J Med Chem , vol.47 , pp. 3131-3141
    • Nam, N.H.1    Ye, G.2    Sun, G.3    Parang, K.4
  • 12
    • 0025739156 scopus 로고
    • Simulated annealing approach to the study ofprotein structures
    • Chou KC, Carlacci L (1991) Simulated annealing approach to the study ofprotein structures. Protein Eng 4: 661-667.
    • (1991) Protein Eng , vol.4 , pp. 661-667
    • Chou, K.C.1    Carlacci, L.2
  • 13
    • 84986505816 scopus 로고
    • Conformational memories and a simulated annealingprogram that learns: Application to LTB4
    • Guarnieri FWS (1995) Conformational memories and a simulated annealingprogram that learns: application to LTB4. J Comput Chem 16: 648-653.
    • (1995) J Comput Chem , vol.16 , pp. 648-653
    • Guarnieri, F.W.S.1
  • 14
    • 0035811239 scopus 로고    scopus 로고
    • A general screened Coulomb potential based implicitsolvent model: Calculation of secondary structures of small peptides
    • Hassan SAME (2001) A general screened Coulomb potential based implicitsolvent model: Calculation of secondary structures of small peptides.Internat J Quant Chem 83: 193-202.
    • (2001) Internat J Quant Chem , vol.83 , pp. 193-202
    • Hassan, S.A.M.E.1
  • 15
    • 10344264957 scopus 로고    scopus 로고
    • Exploring peptide energy landscapes: A test of force fieldsand implicit solvent models
    • Steinbach PJ (2004) Exploring peptide energy landscapes: a test of force fieldsand implicit solvent models. Proteins 57: 665-677.
    • (2004) Proteins , vol.57 , pp. 665-677
    • Steinbach, P.J.1
  • 16
    • 33749235649 scopus 로고    scopus 로고
    • Comparative study of eight oxytocin antagonists bysimulated annealing
    • Jojart B, Marki A (2006) Comparative study of eight oxytocin antagonists bysimulated annealing. J Mol Model 12: 823-828.
    • (2006) J Mol Model , vol.12 , pp. 823-828
    • Jojart, B.1    Marki, A.2
  • 18
    • 27144475507 scopus 로고    scopus 로고
    • Investigation of the binding determinants of phosphopeptides targeted to theSRC homology 2 domain of the signal transducer and activator of transcription3. Development of a high-affinity peptide inhibitor
    • Coleman DRt, Ren Z, Mandal PK, Cameron AG, Dyer GA, et al. (2005) Investigation of the binding determinants of phosphopeptides targeted to theSRC homology 2 domain of the signal transducer and activator of transcription3. Development of a high-affinity peptide inhibitor. J Med Chem 48:6661-6670.
    • (2005) J Med Chem , vol.48 , pp. 6661-6670
    • Coleman, D.1    Ren, Z.2    Mandal, P.K.3    Cameron, A.G.4    Dyer, G.A.5
  • 19
    • 0033638441 scopus 로고    scopus 로고
    • Structural basis for specificity switching of the Src SH2 domain
    • Kimber MS, Nachman J, Cunningham AM, Gish GD, Pawson T, et al. (2000) Structural basis for specificity switching of the Src SH2 domain. Mol Cell 5:1043-1049.
    • (2000) Mol Cell , vol.5 , pp. 1043-1049
    • Kimber, M.S.1    Nachman, J.2    Cunningham, A.M.3    Gish, G.D.4    Pawson, T.5
  • 22
    • 84988053694 scopus 로고
    • An All Atom Force Fieldfor Simulations of Proteins and Nucleic Acids
    • Weiner SJ, Kollman PA, Nguyen DT, Case DA (1986) An All Atom Force Fieldfor Simulations of Proteins and Nucleic Acids. J Comput Chem 7: 230-252.
    • (1986) J Comput Chem , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 23
    • 84986516411 scopus 로고
    • Application of themultimolecule and multiconformational RESP methodology to biopolymers:Charge derivation for DNA, RNA, and proteins
    • Cieplak P, Cornell WD, Bayly CI, Kollman PA (1995) Application of themultimolecule and multiconformational RESP methodology to biopolymers:Charge derivation for DNA, RNA, and proteins. J Comput Chem 16:1357-1377.
    • (1995) J Comput Chem , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Cornell, W.D.2    Bayly, C.I.3    Kollman, P.A.4
  • 25
    • 33748545144 scopus 로고
    • The influence of polarization enenrgies onmolecular orbital hydrogenation energies
    • Hariharan PC, Pople JA (1973) The influence of polarization enenrgies onmolecular orbital hydrogenation energies. Theo Chim Acta 28: 213-222.
    • (1973) Theo Chim Acta , vol.28 , pp. 213-222
    • Hariharan, P.C.1    Pople, J.A.2
  • 26
    • 0033447703 scopus 로고    scopus 로고
    • Solution conformations of structuredpeptides; continuum electrostatiocs versus distance-dependent dielectric functions
    • Schaefer MBC, Karplus M (1999) Solution conformations of structuredpeptides; continuum electrostatiocs versus distance-dependent dielectric functions.Thoer Chem Acc 101: 194-204.
    • (1999) Thoer Chem Acc , vol.101 , pp. 194-204
    • Schaefer, M.B.C.1    Karplus, M.2
  • 27
    • 0029831680 scopus 로고    scopus 로고
    • An automated approach forclustering an ensemble of NMR-derived protein structures into conformationallyrelated subfamilies
    • Kelley LA, Gardner SP, Sutcliffe MJ (1996) An automated approach forclustering an ensemble of NMR-derived protein structures into conformationallyrelated subfamilies. Protein Eng 9: 1063-1065.
    • (1996) Protein Eng , vol.9 , pp. 1063-1065
    • Kelley, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 29
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-srccomplexed with tyrosine-phosphorylated peptides
    • Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, et al. (1992) Crystal structure of the phosphotyrosine recognition domain SH2 of v-srccomplexed with tyrosine-phosphorylated peptides. Nature 358: 646-653.
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1    Kominos, D.2    Robertson, S.C.3    Pant, N.4    Baltimore, D.5
  • 30
    • 15844398102 scopus 로고    scopus 로고
    • Structural basis for specificity of Grb2-SH2 revealed by a novel ligand bindingmode
    • 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 bindingmode. 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
  • 31
    • 0037011907 scopus 로고    scopus 로고
    • Hierarchy of simulation models in predicting structure and energetics of the SrcSH2 domain binding to tyrosyl phosphopeptides
    • Verkhivker GM, Bouzida D, Gehlhaar DK, Rejto PA, Schaffer L, et al. (2002) Hierarchy of simulation models in predicting structure and energetics of the SrcSH2 domain binding to tyrosyl phosphopeptides. J Med Chem 45: 72-89.
    • (2002) J Med Chem , vol.45 , pp. 72-89
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Schaffer, L.5
  • 33
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimentalstudies of peptides and proteins
    • Pace CN, Scholtz JM (1998) A helix propensity scale based on experimentalstudies of peptides and proteins. Biophys J 75: 422-427.
    • (1998) Biophys J , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 34
    • 47249128045 scopus 로고    scopus 로고
    • Areexamination of the propensities of amino acids towards a particular secondarystructure: Classification of amino acids based on their chemical structure
    • Malkov SN, Zivkovic MV, Beljanski MV, Hall MB, Zaric SD (2008) Areexamination of the propensities of amino acids towards a particular secondarystructure: classification of amino acids based on their chemical structure. J MolModel 14: 769-775.
    • (2008) J MolModel , vol.14 , pp. 769-775
    • Malkov, S.N.1    Zivkovic, M.V.2    Beljanski, M.V.3    Hall, M.B.4    Zaric, S.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.