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Volumn 332, Issue 1, 2003, Pages 195-204

The functional binding epitope of a high affinity variant of human growth hormone mapped by shotgun alanine-scanning mutagenesis: Insights into the mechanisms responsible for improved affinity

Author keywords

Alanine scanning; Combinatorial mutagenesis; Phage display; Protein protein interactions; Shotgun scanning

Indexed keywords

ALANINE; EPITOPE; GROWTH HORMONE; GROWTH HORMONE RECEPTOR;

EID: 0043237620     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00898-2     Document Type: Article
Times cited : (42)

References (34)
  • 4
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham B.C., Wells J.A. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science. 244:1989;1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 5
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham B.C., Ultsch M.H., de Vos A.M., Mulkerrin M.G., Clauser K.R., Wells J.A. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science. 254:1991;821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.H.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 6
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • Cunningham B.C., Wells J.A. Comparison of a structural and a functional epitope. J. Mol. Biol. 234:1993;554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 7
    • 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
  • 8
    • 0030707656 scopus 로고    scopus 로고
    • Structural plasticity in a remodeled protein-protein interface
    • Atwell S., Ultsch M.H., de Vos A.M., Wells J.A. Structural plasticity in a remodeled protein-protein interface. Science. 278:1997;1125-1128.
    • (1997) Science , vol.278 , pp. 1125-1128
    • Atwell, S.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 9
    • 0031057518 scopus 로고    scopus 로고
    • The role of receptor dimerization domain residues in growth hormone signaling
    • Chen C., Brinkworth R., Waters M.J. The role of receptor dimerization domain residues in growth hormone signaling. J. Biol. Chem. 272:1997;5133-5140.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5133-5140
    • Chen, C.1    Brinkworth, R.2    Waters, M.J.3
  • 10
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity
    • Clackson T., Ultsch M.H., Wells J.A., de Vos A.M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277:1998;1111-1128.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    De Vos, A.M.4
  • 11
    • 0026598960 scopus 로고
    • Human growth hormone and the extracellular domain of its receptor: Crystal structure of the complex
    • de Vos A.M., Ultsch M.H., Kossiakoff A.A. Human growth hormone and the extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.H.2    Kossiakoff, A.A.3
  • 12
    • 0025214021 scopus 로고
    • Engineering human prolactin to bind to the human growth hormone receptor
    • Cunningham B.C., Henner D.J., Wells J.A. Engineering human prolactin to bind to the human growth hormone receptor. Science. 247:1990;1461-1465.
    • (1990) Science , vol.247 , pp. 1461-1465
    • Cunningham, B.C.1    Henner, D.J.2    Wells, J.A.3
  • 13
    • 0026335990 scopus 로고
    • Rational design of receptor-specific variants of human growth hormone
    • Cunningham B.C., Wells J.A. Rational design of receptor-specific variants of human growth hormone. Proc. Natl Acad. Sci. USA. 88:1991;3407-3411.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3407-3411
    • Cunningham, B.C.1    Wells, J.A.2
  • 14
    • 0026343486 scopus 로고
    • Selecting high-affinity binding proteins by monovalent phage display
    • Lowman H.B., Bass S.H., Simpson N., Wells J.A. Selecting high-affinity binding proteins by monovalent phage display. Biochemistry. 30:1991;10832-10838.
    • (1991) Biochemistry , vol.30 , pp. 10832-10838
    • Lowman, H.B.1    Bass, S.H.2    Simpson, N.3    Wells, J.A.4
  • 15
    • 0029794909 scopus 로고    scopus 로고
    • Structural and mutational analysis of affinity-inert contact residues at the growth hormone-receptor interface
    • Pearce K.H.J., Ultsch M.H., Kelly R.F., de Vos A.M., Wells J.A. Structural and mutational analysis of affinity-inert contact residues at the growth hormone-receptor interface. Biochemistry. 35:1996;10300-10307.
    • (1996) Biochemistry , vol.35 , pp. 10300-10307
    • Pearce, K.H.J.1    Ultsch, M.H.2    Kelly, R.F.3    De Vos, A.M.4    Wells, J.A.5
  • 16
    • 0022721745 scopus 로고
    • Structural features of prolactins and growth hormones that can be related to their biological properties
    • Nicoll C.S., Mayer G.L., Russel S.M. Structural features of prolactins and growth hormones that can be related to their biological properties. Endocrine Rev. 7:1986;169-203.
    • (1986) Endocrine Rev. , vol.7 , pp. 169-203
    • Nicoll, C.S.1    Mayer, G.L.2    Russel, S.M.3
  • 17
    • 0029785849 scopus 로고    scopus 로고
    • Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization
    • Gertler A., Grosclaude J., Strasburger C.J., Nir S., Dijane J. Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization. J. Biol. Chem. 271:1996;24482-24491.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24482-24491
    • Gertler, A.1    Grosclaude, J.2    Strasburger, C.J.3    Nir, S.4    Dijane, J.5
  • 18
    • 0029825056 scopus 로고    scopus 로고
    • Sequence-function relationships within the expanding family of prolactin, growth hormone, placental lactogen, and related proteins in mammals
    • Goffin V., Shiverick K.T., Kelly P.A., Martial J.A. Sequence-function relationships within the expanding family of prolactin, growth hormone, placental lactogen, and related proteins in mammals. Endocrine Rev. 17:1996;385-410.
    • (1996) Endocrine Rev. , vol.17 , pp. 385-410
    • Goffin, V.1    Shiverick, K.T.2    Kelly, P.A.3    Martial, J.A.4
  • 20
    • 0028032203 scopus 로고
    • The X-ray structure of the growth hormone-prolactin receptor complex
    • Somers W., Ultsch M.H., de Vos A.M., Kossiakoff A.A. The X-ray structure of the growth hormone-prolactin receptor complex. Nature. 372:1994;478-481.
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.H.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 22
    • 0027136111 scopus 로고
    • Affinity maturation of human growth hormone: Monovalent phage display
    • Lowman H.B., Wells J.A. Affinity maturation of human growth hormone: monovalent phage display. J. Mol. Biol. 234:1993;564-578.
    • (1993) J. Mol. Biol. , vol.234 , pp. 564-578
    • Lowman, H.B.1    Wells, J.A.2
  • 23
    • 0036289017 scopus 로고    scopus 로고
    • Structure of a phage display-derived variant of human growth hormone complexed to two copies of the extracellular domain of its receptor: Evidence for strong structural coupling between receptor binding sites
    • Schiffer C., Ultsch M., Walsh S., Somers W., de Vos A.M., Kossiakoff A. Structure of a phage display-derived variant of human growth hormone complexed to two copies of the extracellular domain of its receptor: evidence for strong structural coupling between receptor binding sites. J. Mol. Biol. 316:2002;277-289.
    • (2002) J. Mol. Biol. , vol.316 , pp. 277-289
    • Schiffer, C.1    Ultsch, M.2    Walsh, S.3    Somers, W.4    De Vos, A.M.5    Kossiakoff, A.6
  • 25
    • 0037470140 scopus 로고    scopus 로고
    • Origins of PDZ domain ligand specificity: Structure determination and mutagenesis of the Erbin PDZ domain
    • Skelton N.J., Koehler M.F.T., Zobel K., Wong W.L., Yeh S., Pisabarro M.T., et al. Origins of PDZ domain ligand specificity: structure determination and mutagenesis of the Erbin PDZ domain. J. Biol. Chem. 278:2003;7645-7654.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7645-7654
    • Skelton, N.J.1    Koehler, M.F.T.2    Zobel, K.3    Wong, W.L.4    Yeh, S.5    Pisabarro, M.T.6
  • 26
    • 0036295439 scopus 로고    scopus 로고
    • Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis
    • Vajdos F.F., Adams C.W., Breece T.N., Presta L.G., de Vos A.M., Sidhu S.S. Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. J. Mol. Biol. 320:2002;415-428.
    • (2002) J. Mol. Biol. , vol.320 , pp. 415-428
    • Vajdos, F.F.1    Adams, C.W.2    Breece, T.N.3    Presta, L.G.4    De Vos, A.M.5    Sidhu, S.S.6
  • 27
    • 0028217202 scopus 로고
    • The crystal structure of affinity-matured growth hormone at 2 Å resolution
    • Ultsch M.H., Somers W., Kossiakoff A.A., de Vos A.M. The crystal structure of affinity-matured growth hormone at 2 Å resolution. J. Mol. Biol. 236:1994;286-299.
    • (1994) J. Mol. Biol. , vol.236 , pp. 286-299
    • Ultsch, M.H.1    Somers, W.2    Kossiakoff, A.A.3    De Vos, A.M.4
  • 29
    • 0026675750 scopus 로고
    • High resolution functional analysis of antibody-antigen interactions
    • Jin L., Fendly B.M., Wells J.A. High resolution functional analysis of antibody-antigen interactions. J. Mol. Biol. 226:1992;851-865.
    • (1992) J. Mol. Biol. , vol.226 , pp. 851-865
    • Jin, L.1    Fendly, B.M.2    Wells, J.A.3
  • 30
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells J.A. Additivity of mutational effects in proteins. Biochemistry. 29:1990;8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 31
    • 0032875696 scopus 로고    scopus 로고
    • Defining epitopes: It's not as easy as it seems
    • Greenspan N.S., Di Cera E. Defining epitopes: it's not as easy as it seems. Nature Biotechnol. 17:1999;936-937.
    • (1999) Nature Biotechnol. , vol.17 , pp. 936-937
    • Greenspan, N.S.1    Di Cera, E.2
  • 32
    • 0000164734 scopus 로고    scopus 로고
    • Site-specific thermodynamics: Understanding cooperativity in molecular recognition
    • Di Cera E. Site-specific thermodynamics: understanding cooperativity in molecular recognition. Chem. Rev. 98:1998;1563-1591.
    • (1998) Chem. Rev. , vol.98 , pp. 1563-1591
    • Di Cera, E.1
  • 33
    • 0035986872 scopus 로고    scopus 로고
    • Functional promiscuity of squirrel monkey growth receptor toward both primate and non-primate growth hormone
    • Yi S., Bernat B., Pal G., Kossiakoff A., Li W. Functional promiscuity of squirrel monkey growth receptor toward both primate and non-primate growth hormone. Mol. Biol. Evol. 19:2002;1083-1092.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1083-1092
    • Yi, S.1    Bernat, B.2    Pal, G.3    Kossiakoff, A.4    Li, W.5
  • 34
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A., Roberts J.D., Zakour R.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.