메뉴 건너뛰기




Volumn 34, Issue , 2005, Pages 1-20

A quiet life with proteins

Author keywords

Crystallography; Function; Polynucleotides; Structure

Indexed keywords

ANTIBODY; ASPARTIC PROTEINASE; GUANOSINE PHOSPHATE; IMMUNOGLOBULIN F(AB) FRAGMENT; INTEGRASE; LYSOZYME; MONOMER; MYOGLOBIN; POLYADENYLIC ACID; POLYNUCLEOTIDE; PROTEIN; TRYPTOPHAN SYNTHASE;

EID: 20544465416     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.34.040204.144531     Document Type: Review
Times cited : (3)

References (42)
  • 1
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution
    • Amit AG, Mariuzza RA, Phillips SE, Poljak RJ. 1986. Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233:747-53
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.3    Poljak, R.J.4
  • 3
    • 0002590170 scopus 로고
    • A relation between the signs of structure factors
    • 2a. Cochran W. 1952. A relation between the signs of structure factors. Acta Crystallogr. 5:65-67
    • (1952) Acta Crystallogr. , vol.5 , pp. 65-67
    • Cochran, W.1
  • 4
    • 0001704671 scopus 로고
    • The structure of synthetic polypeptides. 1. The transform of atoms on a helix
    • 2b. Cochran W, Crick FHC, Vand V. 1952. The structure of synthetic polypeptides. 1. The transform of atoms on a helix. Acta Crystallogr. 5:581-86
    • (1952) Acta Crystallogr. , vol.5 , pp. 581-586
    • Cochran, W.1    Crick, F.H.C.2    Vand, V.3
  • 6
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • Daopin S, Piez KA, Ogawa Y, Davies DR. 1992. Crystal structure of transforming growth factor-β2: an unusual fold for the superfamily. Science 257:369-73
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 7
    • 20544469081 scopus 로고
    • Polyinosinic plus polycytidylic acid: A crystalline polynucleotide complex
    • Davies DR. 1960. Polyinosinic plus polycytidylic acid: a crystalline polynucleotide complex. Nature 196:1030-31
    • (1960) Nature , vol.196 , pp. 1030-1031
    • Davies, D.R.1
  • 8
    • 0001533214 scopus 로고
    • The crystal structure of parabanic acid
    • Davies DR, Blum JJ. 1955. The crystal structure of parabanic acid. Acta Crystallogr. 8:129-36
    • (1955) Acta Crystallogr. , vol.8 , pp. 129-136
    • Davies, D.R.1    Blum, J.J.2
  • 9
    • 4243735395 scopus 로고
    • A refinement of the crystal structure of succinamide
    • Davies DR, Pasternak R. 1956. A refinement of the crystal structure of succinamide. Acta Crystallogr. 9:334-40
    • (1956) Acta Crystallogr. , vol.9 , pp. 334-340
    • Davies, D.R.1    Pasternak, R.2
  • 10
    • 0000822995 scopus 로고
    • On the importance of being ionized
    • 7a. Davis BD. 1958. On the importance of being ionized. Arch. Biochem. Biophys. 78: 497-509
    • (1958) Arch. Biochem. Biophys. , vol.78 , pp. 497-509
    • Davis, B.D.1
  • 11
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase reveals similarity with other polynucleotidyl transferases
    • Dyda F, Hickman A, Jenkins T, Engelman A, Craigie R, Davies DR. 1994. Crystal structure of the catalytic domain of HIV-1 integrase reveals similarity with other polynucleotidyl transferases. Science 266:1981-86
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.2    Jenkins, T.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 12
    • 33947470407 scopus 로고
    • Formation of a three-stranded polynucleotide molecule
    • Felsenfeld G, Davies DR, Rich A. 1957. Formation of a three-stranded polynucleotide molecule. J. Am. Chem. Soc. 79: 2023-24
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 2023-2024
    • Felsenfeld, G.1    Davies, D.R.2    Rich, A.3
  • 14
    • 13044295993 scopus 로고    scopus 로고
    • Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: A platform for antiviral drug design
    • Goldgur Y, Craigie R, Cohen GH, Fujiwara T, Yoshinaga T, et al. 1999. Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design. Proc. Natl. Acad. Sci. USA 96:13040-43
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13040-13043
    • Goldgur, Y.1    Craigie, R.2    Cohen, G.H.3    Fujiwara, T.4    Yoshinaga, T.5
  • 16
    • 2742615645 scopus 로고
    • Crystal-structure determination by means of a statistical distribution of interatomic vectors
    • 12a. Hauptman H, Karle J. 1952. Crystal-structure determination by means of a statistical distribution of interatomic vectors. Acta Crystallogr. 5:48-59
    • (1952) Acta Crystallogr. , vol.5 , pp. 48-59
    • Hauptman, H.1    Karle, J.2
  • 17
    • 0024297340 scopus 로고
    • Three-dimensional structure of the tryptophan synthase multienzyme complex from Salmonella typhimurium
    • Hyde CD, Padlan EA, Ahmed SA, Miles EW, Davies DR. 1988. Three-dimensional structure of the tryptophan synthase multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263:17857-71
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.D.1    Padlan, E.A.2    Ahmed, S.A.3    Miles, E.W.4    Davies, D.R.5
  • 19
    • 0029075884 scopus 로고
    • The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: Conformational differences with the intact exotoxin
    • Li M, Dyda F, Benhar I, Pastan I, Davies DR. 1995. The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin. Proc. Natl. Acad. Sci. USA 92:9308-12
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9308-9312
    • Li, M.1    Dyda, F.2    Benhar, I.3    Pastan, I.4    Davies, D.R.5
  • 20
    • 0030015488 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of Pseudomonas exotoxin a complexed with a nicotinamide adenine dinucleotide analog: Implications for the activation process and for ADP ribosylation
    • Li M, Dyda F, Benhar I, Pastan I, Davies DR. 1996. Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation. Proc. Natl. Acad. Sci. USA 93:6902-06
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6902-6906
    • Li, M.1    Dyda, F.2    Benhar, I.3    Pastan, I.4    Davies, D.R.5
  • 21
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar transport: Crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: Sugar phosphotransferase system and a model of the phosphotransferase complex with Hpr
    • Liao DI, Silverton E, Seok YJ, Lee BR, Peterkofsky A, Davies DR. 1996. The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransferase complex with Hpr. Structure 4:861-72
    • (1996) Structure , vol.4 , pp. 861-872
    • Liao, D.I.1    Silverton, E.2    Seok, Y.J.3    Lee, B.R.4    Peterkofsky, A.5    Davies, D.R.6
  • 22
    • 0032518247 scopus 로고    scopus 로고
    • Crystal structure of the NAD complex of human deoxyhypusine synthase: An enzyme with a ball and chain mechanism for bloc king the active site
    • Liao DI, Wolff E, Park MH, Davies DR. 1998. Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball and chain mechanism for bloc king the active site. Structure 6:23-32
    • (1998) Structure , vol.6 , pp. 23-32
    • Liao, D.I.1    Wolff, E.2    Park, M.H.3    Davies, D.R.4
  • 23
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J. Mol. Biol. 33:491-97
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 24
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles E, Rhee S, Davies DR. 1999. The molecular basis of substrate channeling. J. Biol. Chem. 274:12193-96
    • (1999) J. Biol. Chem. , vol.274 , pp. 12193-12196
    • Miles, E.1    Rhee, S.2    Davies, D.R.3
  • 26
    • 33947463091 scopus 로고
    • A new twostranded helical structure: Polyadenylic acid and polyuridylic acid
    • Rich A, Davies DR. 1956. A new twostranded helical structure: polyadenylic acid and polyuridylic acid. J. Am. Chem. Soc. 78:3548-49
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 3548-3549
    • Rich, A.1    Davies, D.R.2
  • 27
    • 0033592955 scopus 로고    scopus 로고
    • Structure of a triple helical DNA with a triplex-duplex junction
    • Rhee S, Han Z-J, Liu K, Miles HT, Davies DR. 1999. Structure of a triple helical DNA with a triplex-duplex junction. Biochemistry 38:16810-15
    • (1999) Biochemistry , vol.38 , pp. 16810-16815
    • Rhee, S.1    Han, Z.-J.2    Liu, K.3    Miles, H.T.4    Davies, D.R.5
  • 28
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif of MarA: The first structure for an AraC family transcriptional activator
    • Rhee S, Martin RG, Rosner JL, Davies DR. 1998. A novel DNA-binding motif of MarA: the first structure for an AraC family transcriptional activator. Proc. Natl. Acad. Sci. USA 95:10413-18
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4
  • 31
    • 0000433074 scopus 로고
    • The squaring method: A new method for phase determination
    • 26a. Sayre D. 1952. The squaring method: a new method for phase determination. Acta Crystallogr. 5:60-65
    • (1952) Acta Crystallogr. , vol.5 , pp. 60-65
    • Sayre, D.1
  • 32
    • 0013484210 scopus 로고
    • The three-dimensional structure of a phosphorylcholine binding mouse immunoglobulin Fab and the nature of the antigen binding site
    • Segal DM, Padlan EA, Cohen GH, Rudikoff S, Potter M, Davies DR. 1974. The three-dimensional structure of a phosphorylcholine binding mouse immunoglobulin Fab and the nature of the antigen binding site. Proc. Natl. Acad. Sci. USA 71:4298-302
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4298-4302
    • Segal, D.M.1    Padlan, E.A.2    Cohen, G.H.3    Rudikoff, S.4    Potter, M.5    Davies, D.R.6
  • 33
    • 0015243661 scopus 로고
    • The substrate binding site in bovine chymotrypsin AR: A crystallographic study using peptide chloromethyl ketones as site specific inhibitors
    • Segal DM, Power JC, Cohen GH, Davies DR, Wilcox PE. 1971. The substrate binding site in bovine chymotrypsin AR: a crystallographic study using peptide chloromethyl ketones as site specific inhibitors. Biochemistry 10:3728-37
    • (1971) Biochemistry , vol.10 , pp. 3728-3737
    • Segal, D.M.1    Power, J.C.2    Cohen, G.H.3    Davies, D.R.4    Wilcox, P.E.5
  • 36
    • 0008331792 scopus 로고
    • Homology among acid proteases: Comparison of crystal structure at 3 Å resolution of acid proteases from Rhizopus chinensis and Endothia parasitica
    • Subramanian E, Swan IDA, Liu M, Davies DR, Jenkins JA, et al. 1977. Homology among acid proteases: comparison of crystal structure at 3 Å resolution of acid proteases from Rhizopus chinensis and Endothia parasitica. Proc. Natl. Acad. Sci. USA 74:556-59
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 556-559
    • Subramanian, E.1    Swan, I.D.A.2    Liu, M.3    Davies, D.R.4    Jenkins, J.A.5
  • 37
    • 0023660798 scopus 로고
    • Structure and refinement at 1.8 Å resolution of the aspartic proteinase from Rhizopus chinensis
    • Suguna K, Bott RR, Padlan EA, Subramanian E, Sheriff S, et al. 1987. Structure and refinement at 1.8 Å resolution of the aspartic proteinase from Rhizopus chinensis. J. Mol. Biol. 196:877-900
    • (1987) J. Mol. Biol. , vol.196 , pp. 877-900
    • Suguna, K.1    Bott, R.R.2    Padlan, E.A.3    Subramanian, E.4    Sheriff, S.5
  • 38
    • 0023434194 scopus 로고
    • Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: Implications for a mechanism of action
    • Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR. 1987. Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action. Proc. Natl. Acad. Sci. USA 84:7009-13
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7009-7013
    • Suguna, K.1    Padlan, E.A.2    Smith, C.W.3    Carlson, W.D.4    Davies, D.R.5
  • 39
    • 0014423347 scopus 로고
    • Crystallographic studies of a human immunoglobulin
    • Terry WD, Matthews BW, Davies DR. 1968. Crystallographic studies of a human immunoglobulin. Nature 220: 239-41
    • (1968) Nature , vol.220 , pp. 239-241
    • Terry, W.D.1    Matthews, B.W.2    Davies, D.R.3
  • 41
    • 3142543751 scopus 로고    scopus 로고
    • A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme-NAD-inhibitor ternary complex
    • Umland TC, Wolff EC, Park MH, Davies DR. 2004. A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme-NAD-inhibitor ternary complex. J. Biol. Chem. 279:28697-705
    • (2004) J. Biol. Chem. , vol.279 , pp. 28697-28705
    • Umland, T.C.1    Wolff, E.C.2    Park, M.H.3    Davies, D.R.4
  • 42
    • 0002507936 scopus 로고
    • A new analytical method for solving complex crystal structures
    • Zachariasen WH. 1952. A new analytical method for solving complex crystal structures. Acta Crystallogr. 5:68-73
    • (1952) Acta Crystallogr. , vol.5 , pp. 68-73
    • Zachariasen, W.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.