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Volumn 5, Issue 6, 1997, Pages 799-812

Steroid recognition and regulation of hormone action: Crystal structure of testosterone and NADP+ bound to 3α-hydroxysteroid/dihydrodiol dehydrogenase

Author keywords

3 hydroxysteroid dihydrodiol dehydrogenase; Aldo keto reductase; Crystal structure; Steroid hormone recognition; Testosterone

Indexed keywords

ANIMALIA; MAMMALIA;

EID: 0031570663     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00234-7     Document Type: Article
Times cited : (132)

References (57)
  • 1
    • 0025835877 scopus 로고
    • Cloning and sequencing of the cDNAfor rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase
    • Pawlowski, J.E., Huizinga, M. & Penning, T.M. (1991). Cloning and sequencing of the cDNAfor rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. J. Biol. Chem. 266, 8820-8825.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8820-8825
    • Pawlowski, J.E.1    Huizinga, M.2    Penning, T.M.3
  • 2
    • 85030293014 scopus 로고
    • PhD dissertation, The Johns Hopkins University, Baltimore, Maryland
    • Mukharji, I. (1982). Studies on hydroxysteroid dehydrogenases. PhD dissertation, The Johns Hopkins University, Baltimore, Maryland.
    • (1982) Studies on Hydroxysteroid Dehydrogenases
    • Mukharji, I.1
  • 3
    • 0030581692 scopus 로고    scopus 로고
    • Molecular cloning of human type 3 3α-hydroxysteroid dehydrogenase that differs from 20α-hydroxysteroid dehydrogenase by seven amino acids
    • Dufort, I., Soucy, P., Labrie, F. & Luu-The, V. (1996). Molecular cloning of human type 3 3α-hydroxysteroid dehydrogenase that differs from 20α-hydroxysteroid dehydrogenase by seven amino acids. Biochem. Biophys. Res. Comm. 228, 474-479.
    • (1996) Biochem. Biophys. Res. Comm. , vol.228 , pp. 474-479
    • Dufort, I.1    Soucy, P.2    Labrie, F.3    Luu-The, V.4
  • 4
    • 0029091370 scopus 로고
    • Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3α-hydroxysteroid dehydrogenases
    • Khanna, M., Qin, K.-N., Wang, R.W. & Cheng, K.-C. (1995). Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3α-hydroxysteroid dehydrogenases. J. Biol. Chem. 270, 20162-20168.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20162-20168
    • Khanna, M.1    Qin, K.-N.2    Wang, R.W.3    Cheng, K.-C.4
  • 5
    • 0026552524 scopus 로고
    • Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3α-hydroxysteroid dehydrogenase activity
    • Deyashiki, Y., Taniguchi, H., Amano, T., Nakayama, T., Hara, A. & Sawada, H. (1992). Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3α-hydroxysteroid dehydrogenase activity. Biochem. J. 282, 741-746.
    • (1992) Biochem. J. , vol.282 , pp. 741-746
    • Deyashiki, Y.1    Taniguchi, H.2    Amano, T.3    Nakayama, T.4    Hara, A.5    Sawada, H.6
  • 7
    • 0028226789 scopus 로고
    • Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities
    • Bruce, N.C., Willey, D.L., Coulson, A.F.W. & Jeffery, J. (1994). Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities. Biochem. J. 299, 805-811.
    • (1994) Biochem. J. , vol.299 , pp. 805-811
    • Bruce, N.C.1    Willey, D.L.2    Coulson, A.F.W.3    Jeffery, J.4
  • 8
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldo-keto reductase superfamily
    • in press
    • Jez, J.M., Flynn, T.G. & Penning, T.M. (1997). A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 53, in press.
    • (1997) Biochem. Pharmacol. , vol.53
    • Jez, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 9
    • 0028990098 scopus 로고
    • Short-chain dehydrogenases/reductases (SDR)
    • Jornvall, H., et al., & Ghosh, D. (1995). Short-chain dehydrogenases/reductases (SDR). Biochemistry 34, 6003-6013.
    • (1995) Biochemistry , vol.34 , pp. 6003-6013
    • Jornvall, H.1    Ghosh, D.2
  • 11
    • 0029782723 scopus 로고    scopus 로고
    • 3α-Hydroxysteroid oxidoreductase activities in dihydrotestosterone degradation and back-formation in rat prostate and epididymis
    • Span, P.N., Sweep, C.G.J., Benraad, T.J. & Smals, A.G.H. (1996). 3α-Hydroxysteroid oxidoreductase activities in dihydrotestosterone degradation and back-formation in rat prostate and epididymis. J. Steroid Biochem. Molec. Biol. 58, 319-324.
    • (1996) J. Steroid Biochem. Molec. Biol. , vol.58 , pp. 319-324
    • Span, P.N.1    Sweep, C.G.J.2    Benraad, T.J.3    Smals, A.G.H.4
  • 12
    • 0019473604 scopus 로고
    • Changes in dihydrotestosterone metabolism associated with the development of canine benign prostatic hyperplasia
    • Isaacs, J.T. & Coffey, D.S. (1981). Changes in dihydrotestosterone metabolism associated with the development of canine benign prostatic hyperplasia. Endocrinology. 108, 445-453.
    • (1981) Endocrinology , vol.108 , pp. 445-453
    • Isaacs, J.T.1    Coffey, D.S.2
  • 13
    • 0029990372 scopus 로고    scopus 로고
    • 5α-Reduced androgens play a key role in murine parturition
    • Mahendroo, M.S., Cala, K.M. & Russell, D.W. (1996). 5α-Reduced androgens play a key role in murine parturition. Mol. Endocrinol. 10, 380-392.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 380-392
    • Mahendroo, M.S.1    Cala, K.M.2    Russell, D.W.3
  • 14
    • 0028331867 scopus 로고
    • An anion binding site in human aldose reductase: Mechanistic implications for the binding of citrate, cacodylate, and glucose-6-phosphate
    • Harrison, D.H., Bohren, K.M., Ringe, D., Petsko, G.A. & Gabbay, K.H. (1994). An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose-6-phosphate. Biochemistry 33, 2011-2020.
    • (1994) Biochemistry , vol.33 , pp. 2011-2020
    • Harrison, D.H.1    Bohren, K.M.2    Ringe, D.3    Petsko, G.A.4    Gabbay, K.H.5
  • 15
    • 0027378377 scopus 로고
    • Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat
    • Wilson, D.K., Tarle, I., Petrash, J.M. & Quiocho, F.A. (1993). Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc. Natl. Acad. Sci. USA 90, 9847-9851.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9847-9851
    • Wilson, D.K.1    Tarle, I.2    Petrash, J.M.3    Quiocho, F.A.4
  • 16
    • 0028970887 scopus 로고
    • 1.7 Å structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor
    • Wilson, D.K., Nakano, T., Petrash, J.M. & Quiocho, F.A. (1995). 1.7 Å structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry 34, 14323-14330.
    • (1995) Biochemistry , vol.34 , pp. 14323-14330
    • Wilson, D.K.1    Nakano, T.2    Petrash, J.M.3    Quiocho, F.A.4
  • 17
    • 0028269192 scopus 로고
    • Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile acid binder
    • Deyashiki, Y., et al., & Hara, A. (1994). Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile acid binder. Biochem. J. 299, 545-552.
    • (1994) Biochem. J. , vol.299 , pp. 545-552
    • Deyashiki, Y.1    Hara, A.2
  • 18
    • 0027158606 scopus 로고
    • cDNA cloning and expression of the human hepatic bile acid-binding protein
    • Stolz, A., Hammond, L., Lou, H., Takikawa, H., Ronk, M. & Shively, J.E. (1993). cDNA cloning and expression of the human hepatic bile acid-binding protein. J. Biol. Chem. 268, 10448-10457.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10448-10457
    • Stolz, A.1    Hammond, L.2    Lou, H.3    Takikawa, H.4    Ronk, M.5    Shively, J.E.6
  • 19
    • 0030034858 scopus 로고    scopus 로고
    • Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells
    • Hara, A., et al., & Ishida, N.(1996). Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem. J. 313, 373-376.
    • (1996) Biochem. J. , vol.313 , pp. 373-376
    • Hara, A.1    Ishida, N.2
  • 20
    • 0028943455 scopus 로고
    • Molecular cloning and characterization of mouse estradiol 17β-dehydrogenase (A-specific), a member of the aldoketoreductase family
    • Deyashiki, Y., Ohshima, K., Nakanishi, M., Sato, K., Matsuura, K. & Hara, A. (1995). Molecular cloning and characterization of mouse estradiol 17β-dehydrogenase (A-specific), a member of the aldoketoreductase family. J. Biol. Chem. 270, 10461-10467.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10461-10467
    • Deyashiki, Y.1    Ohshima, K.2    Nakanishi, M.3    Sato, K.4    Matsuura, K.5    Hara, A.6
  • 21
    • 0027399542 scopus 로고
    • Molecular cloning and expression of an abundant rabbit ovarian protein with 20α-hydroxysteroid dehydrogenase activity
    • Lacy, W.R., Washenick, K.J., Cook, R.G. & Dunbar, B.S. (1993). Molecular cloning and expression of an abundant rabbit ovarian protein with 20α-hydroxysteroid dehydrogenase activity. Mol. Endocrinol. 7, 58-66.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 58-66
    • Lacy, W.R.1    Washenick, K.J.2    Cook, R.G.3    Dunbar, B.S.4
  • 22
    • 0028212739 scopus 로고
    • Molecular cloning of cDNA for rat ovarian 20α-hydroxysteroid dehydrogenase (HSD1)
    • Miura, R., Shiota, K., Noda, K., Yagi, S., Ogawa, T. & Takahashi, M. (1994). Molecular cloning of cDNA for rat ovarian 20α-hydroxysteroid dehydrogenase (HSD1). Biochem. J. 299, 561-567.
    • (1994) Biochem. J. , vol.299 , pp. 561-567
    • Miura, R.1    Shiota, K.2    Noda, K.3    Yagi, S.4    Ogawa, T.5    Takahashi, M.6
  • 23
    • 0029761692 scopus 로고    scopus 로고
    • Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol
    • Azzi, A., Rehse, P.H., Zhu, D.-W., Campbell, R.L., Labrie, F. & Lin, S.-X. (1996). Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol. Nat. Struct. Biol. 3, 665-668.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 665-668
    • Azzi, A.1    Rehse, P.H.2    Zhu, D.-W.3    Campbell, R.L.4    Labrie, F.5    Lin, S.-X.6
  • 25
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanaka, N., Nonaka, T., Tanabe, T., Yoshimoto, T., Tsuru, D. & Mitsui, Y. (1996). Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35, 7715-7730.
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yoshimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 26
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisited
    • Kleywegt, G.J. & Jones, T.A. (1996). Phi/Psi-chology: Ramachandran revisited. Structure 4, 1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 28
    • 0028274855 scopus 로고
    • Three-dimensional structure of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily
    • Hoog, S.S., Pawlowski, J.E., Alzari, P.M., Penning, T.M. & Lewis, M. (1994). Three-dimensional structure of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc. Natl. Acad. Sci. USA 91, 251 7-2521.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2517-2521
    • Hoog, S.S.1    Pawlowski, J.E.2    Alzari, P.M.3    Penning, T.M.4    Lewis, M.5
  • 29
    • 0029860449 scopus 로고    scopus 로고
    • Characterization of the substrate binding site in rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence
    • Jez, J.M., Schlegel, B.P. & Penning, T.M. (1996). Characterization of the substrate binding site in rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence. J. Biol. Chem. 271, 30190-30198.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30190-30198
    • Jez, J.M.1    Schlegel, B.P.2    Penning, T.M.3
  • 30
    • 0030248351 scopus 로고    scopus 로고
    • Mammalian 3α-hydroxysteroid dehydrogenases
    • Penning, T.M., et al., & Lewis, M.(1996). Mammalian 3α-hydroxysteroid dehydrogenases. Steroids 61, 508-523.
    • (1996) Steroids , vol.61 , pp. 508-523
    • Penning, T.M.1    Lewis, M.2
  • 32
    • 0026443085 scopus 로고
    • The crystal structure of the aldose reductase-NADPH binary complex
    • Borhani, D.W., Harter, T.M. & Petrash, J.M. (1992). The crystal structure of the aldose reductase-NADPH binary complex. J. Biol. Chem. 267, 24841-24847.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24841-24847
    • Borhani, D.W.1    Harter, T.M.2    Petrash, J.M.3
  • 33
    • 0026719692 scopus 로고
    • An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications
    • Wilson, D.K., Bohren, K.M., Gabbay, K.H. & Quiocho, F.A. (1992). An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257, 81-84.
    • (1992) Science , vol.257 , pp. 81-84
    • Wilson, D.K.1    Bohren, K.M.2    Gabbay, K.H.3    Quiocho, F.A.4
  • 34
    • 0025826142 scopus 로고
    • The kinetic mechanism catalysed by homogeneous rat liver 3α-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs
    • Askonas, L.J., Ricigliano, J.W. & Penning, T.M. (1991). The kinetic mechanism catalysed by homogeneous rat liver 3α-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs. Biochem. J. 278, 835-841.
    • (1991) Biochem. J. , vol.278 , pp. 835-841
    • Askonas, L.J.1    Ricigliano, J.W.2    Penning, T.M.3
  • 35
    • 0026531024 scopus 로고
    • Novel NADPH-binding domain revealed by the crystal structure of aldose reductase
    • Rondeau, J.-M., et al., & Moras, D. (1992). Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 355, 469-472.
    • (1992) Nature , vol.355 , pp. 469-472
    • Rondeau, J.-M.1    Moras, D.2
  • 36
    • 0028123784 scopus 로고
    • Studies on pig aldose reductase: Identification of an essential arginine in the primary and tertiary structure of the enzyme
    • Kubiseski, T.J., Green, N.C., Borhani, D.W. & Flynn, T.G. (1994). Studies on pig aldose reductase: identification of an essential arginine in the primary and tertiary structure of the enzyme. J. Biol. Chem. 269, 2183-2188.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2183-2188
    • Kubiseski, T.J.1    Green, N.C.2    Borhani, D.W.3    Flynn, T.G.4
  • 37
    • 0028222097 scopus 로고
    • Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: Enzyme kinetics and crystal structure of the Y48H mutant enzyme
    • Bohren, K.M., et al., & Gabbay, K.H. (1994). Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 33, 2021-2032.
    • (1994) Biochemistry , vol.33 , pp. 2021-2032
    • Bohren, K.M.1    Gabbay, K.H.2
  • 38
    • 0027421590 scopus 로고
    • Bovine lens aldose reductase: PH-dependence of steady-state kinetic parameters and nucleotide binding
    • Liu, S.-Q., Bhatnagar, A. & Srivastava, S.K. (1993). Bovine lens aldose reductase: pH-dependence of steady-state kinetic parameters and nucleotide binding. J. Biol. Chem. 268, 25494-25499.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25494-25499
    • Liu, S.-Q.1    Bhatnagar, A.2    Srivastava, S.K.3
  • 39
    • 0029103124 scopus 로고
    • Mechanism of human aldehyde reductase: Characterization of the active site pocket
    • Barski, O.A., Gabbay, K.H., Grimshaw, C.E. & Bohren, K.M. (1995). Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34, 11264-11275.
    • (1995) Biochemistry , vol.34 , pp. 11264-11275
    • Barski, O.A.1    Gabbay, K.H.2    Grimshaw, C.E.3    Bohren, K.M.4
  • 40
    • 0030458319 scopus 로고    scopus 로고
    • The fascinating complexities of steroid-binding enzymes
    • Duax, W.L., Griffin, J.F. & Ghosh, D. (1996). The fascinating complexities of steroid-binding enzymes. Curr. Opin. Struct. Biol. 6, 813-823.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 813-823
    • Duax, W.L.1    Griffin, J.F.2    Ghosh, D.3
  • 41
    • 0025805084 scopus 로고
    • +-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme
    • +-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem. Biophys. Res. Comm. 176, 840-845.
    • (1991) Biochem. Biophys. Res. Comm. , vol.176 , pp. 840-845
    • Ensor, C.M.1    Tai, H.-H.2
  • 42
    • 0027309435 scopus 로고
    • Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for the involvement of tyrosine-152 and lysine-156 in catalysis
    • Chen, Z., Jiang, J.C., Lin, Z.-G., Lee, W.R., Baker, M.E. & Chang, S.H. (1993). Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for the involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry 32, 3342-3346.
    • (1993) Biochemistry , vol.32 , pp. 3342-3346
    • Chen, Z.1    Jiang, J.C.2    Lin, Z.-G.3    Lee, W.R.4    Baker, M.E.5    Chang, S.H.6
  • 43
    • 0026445622 scopus 로고
    • Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase
    • Obeid, J. & White, P.C. (1992). Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Comm. 188, 222-227.
    • (1992) Biochem. Biophys. Res. Comm. , vol.188 , pp. 222-227
    • Obeid, J.1    White, P.C.2
  • 44
    • 0031021249 scopus 로고    scopus 로고
    • Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions
    • Opperman, U.C.T., et al., & Jornvall, H. (1997). Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions. Biochemistry 36, 34-40.
    • (1997) Biochemistry , vol.36 , pp. 34-40
    • Opperman, U.C.T.1    Jornvall, H.2
  • 45
    • 0027461303 scopus 로고
    • Molecular cloning of testicular 20α-hydroxysteroid dehydrogenase: Identity with aldose reductase
    • Warren, J.C., Murdock, G.L., Ma, Y., Goodman, S.R. & Zimrner, W.E. (1993). Molecular cloning of testicular 20α-hydroxysteroid dehydrogenase: identity with aldose reductase. Biochemistry 32, 1401-1406.
    • (1993) Biochemistry , vol.32 , pp. 1401-1406
    • Warren, J.C.1    Murdock, G.L.2    Ma, Y.3    Goodman, S.R.4    Zimrner, W.E.5
  • 46
  • 47
    • 0022974550 scopus 로고
    • Regio- and stereospecificity of homogeneous 3α-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodial metabolites of polycyclic aromatic hydrocarbons
    • Smithgall, T.E., Harvey, R.G. & Penning, T.M. (1986). Regio- and stereospecificity of homogeneous 3α-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodial metabolites of polycyclic aromatic hydrocarbons. J. Biol. Chem. 261, 6184-6191.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6184-6191
    • Smithgall, T.E.1    Harvey, R.G.2    Penning, T.M.3
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. (1996). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 53
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P. & Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 54
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 55
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 56
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 57
    • 0028057108 scopus 로고
    • Raster 3D version 2.0-a program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. (1994). Raster 3D version 2.0-a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


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