메뉴 건너뛰기




Volumn 11, Issue 6, 2004, Pages 835-844

Molecular recognition properties of FN3 monobodies that bind the Src SH3 domain

Author keywords

[No Author keywords available]

Indexed keywords

CSK PROTEIN, HUMAN; FIBRONECTIN; LIGAND; ONCOPROTEIN; PEPTIDE; PEPTIDE LIBRARY; PHOSPHOTRANSFERASE; PROLINE; PROTEIN TYROSINE KINASE;

EID: 3042633729     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.04.009     Document Type: Article
Times cited : (57)

References (39)
  • 1
    • 0033181011 scopus 로고    scopus 로고
    • Design and expression of soluble CTLA-4 variable domain as a scaffold for the display of functional polypeptides
    • Nuttall S.D., Rousch M.J., Irving R.A., Hufton S.E., Hoogenboom H.R., Hudson P.J. Design and expression of soluble CTLA-4 variable domain as a scaffold for the display of functional polypeptides. Proteins. 36:1999;217-227
    • (1999) Proteins , vol.36 , pp. 217-227
    • Nuttall, S.D.1    Rousch, M.J.2    Irving, R.A.3    Hufton, S.E.4    Hoogenboom, H.R.5    Hudson, P.J.6
  • 2
    • 0028982245 scopus 로고
    • A combinatorial library of an alpha-helical bacterial receptor domain
    • Nord K., Nilsson J., Nilsson B., Uhlen M., Nygren P.A. A combinatorial library of an alpha-helical bacterial receptor domain. Protein Eng. 8:1995;601-608
    • (1995) Protein Eng. , vol.8 , pp. 601-608
    • Nord, K.1    Nilsson, J.2    Nilsson, B.3    Uhlen, M.4    Nygren, P.A.5
  • 3
    • 0033515005 scopus 로고    scopus 로고
    • Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold
    • Beste G., Schmidt F.S., Stibora T., Skerra A. Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc. Natl. Acad. Sci. USA. 96:1999;1898-1903
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1898-1903
    • Beste, G.1    Schmidt, F.S.2    Stibora, T.3    Skerra, A.4
  • 4
    • 0346031536 scopus 로고    scopus 로고
    • Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies
    • Zeytun A., Jeromin A., Scalettar B.A., Waldo G.S., Bradbury A.R. Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies. Nat. Biotechnol. 21:2003;1473-1479
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1473-1479
    • Zeytun, A.1    Jeromin, A.2    Scalettar, B.A.3    Waldo, G.S.4    Bradbury, A.R.5
  • 5
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide A., Bailey C.W., Huang X., Koide S. The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 284:1998;1141-1151
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 6
    • 0036940153 scopus 로고    scopus 로고
    • Exploring the potential of the monobody scaffold: Effects of loop elongation on the stability of a fibronectin type III domain
    • Batori V., Koide A., Koide S. Exploring the potential of the monobody scaffold. effects of loop elongation on the stability of a fibronectin type III domain Protein Eng. 15:2002;1015-1020
    • (2002) Protein Eng. , vol.15 , pp. 1015-1020
    • Batori, V.1    Koide, A.2    Koide, S.3
  • 8
    • 0037022351 scopus 로고    scopus 로고
    • Probing protein conformational changes in living cells by using designer binding proteins: Application to the estrogen receptor
    • Koide A., Abbatiello S., Rothgery L., Koide S. Probing protein conformational changes in living cells by using designer binding proteins. application to the estrogen receptor Proc. Natl. Acad. Sci. USA. 99:2002;1253-1258
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1253-1258
    • Koide, A.1    Abbatiello, S.2    Rothgery, L.3    Koide, S.4
  • 10
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown M.T., Cooper J.A. Regulation, substrates and functions of src. Biochim. Biophys. Acta. 1287:1996;121-149
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 12
    • 0028086395 scopus 로고
    • Regulation of Src family kinases in the developing rat brain: Correlation with their regulator kinase, Csk
    • Inomata M., Takayama Y., Kiyama H., Nada S., Okada M., Nakagawa H. Regulation of Src family kinases in the developing rat brain. correlation with their regulator kinase, Csk J. Biochem. (Tokyo). 116:1994;386-392
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 386-392
    • Inomata, M.1    Takayama, Y.2    Kiyama, H.3    Nada, S.4    Okada, M.5    Nakagawa, H.6
  • 14
    • 0027984955 scopus 로고
    • Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries
    • Sparks A.B., Quilliam L.A., Thorn J.M., Der C.J., Kay B.K. Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries. J. Biol. Chem. 269:1994;23853-23856
    • (1994) J. Biol. Chem. , vol.269 , pp. 23853-23856
    • Sparks, A.B.1    Quilliam, L.A.2    Thorn, J.M.3    Der, C.J.4    Kay, B.K.5
  • 16
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins. SAR by NMR Science. 274:1996;1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 17
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • Feng S., Kasahara C., Rickles R.J., Schreiber S.L. Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc. Natl. Acad. Sci. USA. 92:1995;12408-12415
    • (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
  • 18
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science. 267:1995;383-386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 19
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B.K., Williamson M.P., Sudol M. The importance of being proline. the interaction of proline-rich motifs in signaling proteins with their cognate domains FASEB J. 14:2000;231-241
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 20
    • 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 J.K., Yu H., Simon J.A., Schreiber S.L. Two binding orientations for peptides to the Src SH3 domain. development of a general model for SH3-ligand interactions Science. 266:1994;1241-1247
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 21
  • 23
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D. The three-dimensional structure of the tenth type III module of fibronectin. an insight into RGD-mediated interactions Cell. 71:1992;671-678
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 24
    • 0042129943 scopus 로고    scopus 로고
    • Large antibody display libraries for isolation of high-affinity antibodies
    • Ling M.M. Large antibody display libraries for isolation of high-affinity antibodies. Comb. Chem. High Throughput Screen. 6:2003;421-432
    • (2003) Comb. Chem. High Throughput Screen. , vol.6 , pp. 421-432
    • Ling, M.M.1
  • 25
    • 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 M.A., Zheng J., Cowburn D., Kuriyan J., Saksela K. 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. 14:1995;5006-5015
    • (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    Kuriyan, J.6    Saksela, K.7
  • 26
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2
    • Sparks A.B., Rider J.E., Hoffman N.G., Fowlkes D.M., Quillam L.A., Kay B.K. Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2. Proc. Natl. Acad. Sci. USA. 93:1996;1540-1544
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quillam, L.A.5    Kay, B.K.6
  • 27
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface
    • Koide A., Jordan M.R., Horner S.R., Batori V., Koide S. Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. Biochemistry. 40:2001;10326-10333
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1    Jordan, M.R.2    Horner, S.R.3    Batori, V.4    Koide, S.5
  • 28
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Arbabi Ghahroudi M., Desmyter A., Wyns L., Hamers R., Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 414:1997;521-526
    • (1997) FEBS Lett. , vol.414 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 29
    • 0029972190 scopus 로고    scopus 로고
    • A vancomycin-inducible lacZ reporter system in Bacillus subtilis: Induction by antibiotics that inhibit cell wall synthesis and by lysozyme
    • Ulijasz A.T., Grenader A., Weisblum B. A vancomycin-inducible lacZ reporter system in Bacillus subtilis. induction by antibiotics that inhibit cell wall synthesis and by lysozyme J. Bacteriol. 178:1996;6305-6309
    • (1996) J. Bacteriol. , vol.178 , pp. 6305-6309
    • Ulijasz, A.T.1    Grenader, A.2    Weisblum, B.3
  • 30
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C., de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18:1990;6069-6074
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 31
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D., Kovaleva E., Schatz P.J. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8:1999;921-929
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 32
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 33
    • 0029036496 scopus 로고
    • Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer
    • Zhang O., Forman-Kay J.D. Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer. Biochemistry. 34:1995;6784-6794
    • (1995) Biochemistry , vol.34 , pp. 6784-6794
    • Zhang, O.1    Forman-Kay, J.D.2
  • 35
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. NMRView. A computer program for the visualization and analysis of NMR data J. Biomol. NMR. 4:1994;603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 36
    • 0002608849 scopus 로고
    • Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination
    • Clore G.M., Gronenborn A.M. Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Prog. NMR Spectosc. 23:1991;43-92
    • (1991) Prog. NMR Spectosc. , vol.23 , pp. 43-92
    • Clore, G.M.1    Gronenborn, A.M.2
  • 38
    • 0344541116 scopus 로고    scopus 로고
    • Recent developments for the efficient crystallographic refinement of macromolecular structures
    • Brunger A.T., Adams P.D., Rice L.M. Recent developments for the efficient crystallographic refinement of macromolecular structures. Curr. Opin. Struct. Biol. 8:1998;606-611
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 606-611
    • Brunger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 39
    • 3042594038 scopus 로고    scopus 로고
    • In vivo biotinylated proteins as targets for phage-display selection experiments
    • Scholle M.D., Collart F.R., Kay B.K. In vivo biotinylated proteins as targets for phage-display selection experiments. Protein Expr. Purif. in press:2004
    • (2004) Protein Expr. Purif.
    • Scholle, M.D.1    Collart, F.R.2    Kay, B.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.