메뉴 건너뛰기




Volumn 455, Issue 7212, 2008, Pages 497-502

Crystal structure of opsin in its G-protein-interacting conformation

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; OPSIN;

EID: 52949102889     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07330     Document Type: Article
Times cited : (947)

References (62)
  • 2
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom, M. C. & Schioth, H. B. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nature Rev. Drug Discov. 7, 339-357 (2008).
    • (2008) Nature Rev. Drug Discov , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 3
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada, T., Ernst, O. P., Palczewski, K. & Hofmann, K. P. Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem. Sci. 26, 318-324 (2001).
    • (2001) Trends Biochem. Sci , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 5
    • 2942617209 scopus 로고    scopus 로고
    • Dark adaptation and the retinoid cycle of vision
    • Lamb, T. D. & Pugh, E. N. Jr. Dark adaptation and the retinoid cycle of vision. Prog. Retin. Eye Res. 23, 307-380 (2004).
    • (2004) Prog. Retin. Eye Res , vol.23 , pp. 307-380
    • Lamb, T.D.1    Pugh Jr., E.N.2
  • 6
    • 0035914463 scopus 로고    scopus 로고
    • Conformations of the active and inactive states of opsin
    • Vogel, R. & Siebert, F. Conformations of the active and inactive states of opsin. J. Biol. Chem. 276, 38487-38493 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 38487-38493
    • Vogel, R.1    Siebert, F.2
  • 7
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 9
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T. et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342, 571-583 (2004).
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1
  • 10
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • Murakami, M. & Kouyama, T. Crystal structure of squid rhodopsin. Nature 453, 363-367 (2008).
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 11
    • 33748079137 scopus 로고    scopus 로고
    • Local peptide movement in the photoreaction intermediate of rhodopsin
    • Nakamichi, H. & Okada, T. Local peptide movement in the photoreaction intermediate of rhodopsin. Proc. Natl Acad. Sci. USA 103, 12729-12734 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12729-12734
    • Nakamichi, H.1    Okada, T.2
  • 12
    • 33750836895 scopus 로고    scopus 로고
    • Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
    • Salom, D. et al. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc. Natl Acad. Sci. USA 103, 16123-16128 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16123-16128
    • Salom, D.1
  • 13
    • 47949129742 scopus 로고    scopus 로고
    • 1-adrenergic G-protein-coupled receptor
    • 1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 14
    • 36448995359 scopus 로고    scopus 로고
    • 2-adrenergic G protein-coupled receptor
    • 2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 15
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L. & Khorana, H. G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770 (1996).
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 16
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh, S. P., Zvyaga, T. A., Lichtarge, O., Sakmar, T. P. & Bourne, H. R. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383, 347-350 (1996).
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 17
    • 44949236117 scopus 로고    scopus 로고
    • High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    • Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P.&Hubbell, W. L. High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl Acad. Sci. USA 105, 7439-7444 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 18
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H.-W. & Ernst, O. P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183-187 (2008).
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.-W.4    Ernst, O.P.5
  • 19
    • 0344406765 scopus 로고    scopus 로고
    • 5,6F motif in the rhodopsin ground state and during activation
    • 5,6F motif in the rhodopsin ground state and during activation. Proc. Natl Acad. Sci. USA 100, 2290-2295 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2290-2295
    • Fritze, O.1
  • 20
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the a subunit
    • Hamm, H. E. et al. Site of G protein binding to rhodopsin mapped with synthetic peptides from the a subunit. Science 241, 832-835 (1988).
    • (1988) Science , vol.241 , pp. 832-835
    • Hamm, H.E.1
  • 21
    • 0028093624 scopus 로고
    • A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling
    • Kisselev, O. G., Ermolaeva, M. V. & Gautam, N. A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling. J. Biol. Chem. 269, 21399-21402 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 22
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham, W. M. & Hamm, H. E. Heterotrimeric G protein activation by G-protein-coupled receptors. Nature Rev. Mol. Cell Biol. 9, 60-71 (2008).
    • (2008) Nature Rev. Mol. Cell Biol , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 23
    • 2642588172 scopus 로고    scopus 로고
    • Sequence of interactions in receptor-G protein coupling
    • Herrmann, R. et al. Sequence of interactions in receptor-G protein coupling. J. Biol. Chem. 279, 24283-24290 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 24283-24290
    • Herrmann, R.1
  • 24
    • 0032516098 scopus 로고    scopus 로고
    • Light-activated rhodopsin induces structural binding motif in G protein α subunit
    • Kisselev, O. G. et al. Light-activated rhodopsin induces structural binding motif in G protein α subunit. Proc. Natl Acad. Sci. USA 95, 4270-4275 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4270-4275
    • Kisselev, O.G.1
  • 25
    • 0036385914 scopus 로고    scopus 로고
    • Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
    • Koenig, B. W. et al. Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. J. Mol. Biol. 322, 441-461 (2002).
    • (2002) J. Mol. Biol , vol.322 , pp. 441-461
    • Koenig, B.W.1
  • 26
    • 0027317273 scopus 로고
    • Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state
    • Arnis, S. & Hofmann, K. P. Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc. Natl Acad. Sci. USA 90, 7849-7853 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7849-7853
    • Arnis, S.1    Hofmann, K.P.2
  • 27
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Arnis, S., Fahmy, K., Hofmann, K. P. & Sakmar, T. P. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 269, 23879-23881 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 23879-23881
    • Arnis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 28
    • 0030975286 scopus 로고    scopus 로고
    • Transducin-α C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin
    • Acharya, S., Saad, Y. & Karnik, S. S. Transducin-α C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin. J. Biol. Chem. 272, 6519-6524 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 6519-6524
    • Acharya, S.1    Saad, Y.2    Karnik, S.S.3
  • 29
    • 3142773613 scopus 로고    scopus 로고
    • Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus
    • Janz, J. M. & Farrens, D. L. Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus. J. Biol. Chem. 279, 29767-29773 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 29767-29773
    • Janz, J.M.1    Farrens, D.L.2
  • 30
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent
    • Cai, K., Itoh, Y. & Khorana, H. G. Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent. Proc. Natl Acad. Sci. USA 98, 4877-4882 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 31
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of a heterotrimeric G protein
    • Lambright, D. G. et al. The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379, 311-319 (1996).
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1
  • 32
    • 33646379375 scopus 로고    scopus 로고
    • Conformational changes associated with receptor stimulated guanine nucleotide exchange in a heterotrimeric G-protein α-subunit: NMR analysis of GTPγ S-bound states
    • Ridge, K. D. et al. Conformational changes associated with receptor stimulated guanine nucleotide exchange in a heterotrimeric G-protein α-subunit: NMR analysis of GTPγ S-bound states. J. Biol. Chem. 281, 7635-7648 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 7635-7648
    • Ridge, K.D.1
  • 33
    • 0034695482 scopus 로고    scopus 로고
    • Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits
    • Ernst, O. P. et al. Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits. J. Biol. Chem. 275, 1937-1943 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 1937-1943
    • Ernst, O.P.1
  • 34
    • 20144372892 scopus 로고    scopus 로고
    • Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel
    • Edwards, M. D. et al. Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel. Nature Struct. Mol. Biol. 12, 113-119 (2005).
    • (2005) Nature Struct. Mol. Biol , vol.12 , pp. 113-119
    • Edwards, M.D.1
  • 35
    • 44049094995 scopus 로고    scopus 로고
    • Hydrogen-bonding and packing features of membrane proteins: Functional implications
    • Hildebrand, P. W. et al. Hydrogen-bonding and packing features of membrane proteins: functional implications. Biophys. J. 94, 1945-1953 (2008).
    • (2008) Biophys. J , vol.94 , pp. 1945-1953
    • Hildebrand, P.W.1
  • 36
    • 0027050784 scopus 로고
    • Mechanism of activation and inactivation of opsin: Role of Glu 113 and Lys 296
    • Cohen, G. B., Oprian, D. D. & Robinson, P. R. Mechanism of activation and inactivation of opsin: role of Glu 113 and Lys 296. Biochemistry 31, 12592-12601 (1992).
    • (1992) Biochemistry , vol.31 , pp. 12592-12601
    • Cohen, G.B.1    Oprian, D.D.2    Robinson, P.R.3
  • 37
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • De Lean, A., Stadel, J. M. & Lefkowitz, R. J. A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor. J. Biol. Chem. 255, 7108-7117 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 38
    • 0027270898 scopus 로고
    • Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group
    • Fahmy, K. & Sakmar, T. P. Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32, 7229-7236 (1993).
    • (1993) Biochemistry , vol.32 , pp. 7229-7236
    • Fahmy, K.1    Sakmar, T.P.2
  • 39
    • 0025036350 scopus 로고
    • Rhodopsin mutants that bind but fail to activate transducin
    • Franke, R. R., König, B., Sakmar, T. P., Khorana, H. G. & Hofmann, K. P. Rhodopsin mutants that bind but fail to activate transducin. Science 250, 123-125 (1990).
    • (1990) Science , vol.250 , pp. 123-125
    • Franke, R.R.1    König, B.2    Sakmar, T.P.3    Khorana, H.G.4    Hofmann, K.P.5
  • 41
    • 0040141552 scopus 로고    scopus 로고
    • Signaling states of rhodopsin. Retinal provides a scaffold for activating proton transfer switches
    • Meyer, C. K. et al. Signaling states of rhodopsin. Retinal provides a scaffold for activating proton transfer switches. J. Biol. Chem. 275, 19713-19718 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 19713-19718
    • Meyer, C.K.1
  • 42
    • 0035046325 scopus 로고    scopus 로고
    • Role of noncovalent binding of 11-cis-retinal to opsin in dark adaptation of rod and cone photoreceptors
    • Kefalov, V. J., Crouch, R. K. & Cornwall, M. C. Role of noncovalent binding of 11-cis-retinal to opsin in dark adaptation of rod and cone photoreceptors. Neuron 29, 749-755 (2001).
    • (2001) Neuron , vol.29 , pp. 749-755
    • Kefalov, V.J.1    Crouch, R.K.2    Cornwall, M.C.3
  • 44
    • 0035085209 scopus 로고    scopus 로고
    • Probing the mechanism of rhodopsin-catalyzed transducin activation
    • Natochin, M., Moussaif, M. & Artemyev, N. O. Probing the mechanism of rhodopsin-catalyzed transducin activation. J. Neurochem. 77, 202-210 (2001).
    • (2001) J. Neurochem , vol.77 , pp. 202-210
    • Natochin, M.1    Moussaif, M.2    Artemyev, N.O.3
  • 45
    • 0037018839 scopus 로고    scopus 로고
    • Disruption of the α5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange
    • Marin, E. P., Krishna, A. G. & Sakmar, T. P. Disruption of the α5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange. Biochemistry 41, 6988-6994 (2002).
    • (2002) Biochemistry , vol.41 , pp. 6988-6994
    • Marin, E.P.1    Krishna, A.G.2    Sakmar, T.P.3
  • 46
    • 33749546642 scopus 로고    scopus 로고
    • Signal transfer from GPCRs to G proteins: Role of the Gα N-terminal region in rhodopsin-transducin coupling
    • Herrmann, R., Heck, M., Henklein, P., Hofmann, K. P. & Ernst, O. P. Signal transfer from GPCRs to G proteins: Role of the Gα N-terminal region in rhodopsin-transducin coupling. J. Biol. Chem. 281, 30234-30241 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 30234-30241
    • Herrmann, R.1    Heck, M.2    Henklein, P.3    Hofmann, K.P.4    Ernst, O.P.5
  • 47
    • 30044447642 scopus 로고    scopus 로고
    • The carboxyl terminus of the Gα-subunit is the latch for triggered activation of heterotrimeric G proteins
    • Nanoff, C. et al. The carboxyl terminus of the Gα-subunit is the latch for triggered activation of heterotrimeric G proteins. Mol. Pharmacol. 69, 397-405 (2006).
    • (2006) Mol. Pharmacol , vol.69 , pp. 397-405
    • Nanoff, C.1
  • 49
    • 0035971240 scopus 로고    scopus 로고
    • Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism
    • Heck, M. & Hofmann, K. P. Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism. J. Biol. Chem. 276, 10000-10009 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 10000-10009
    • Heck, M.1    Hofmann, K.P.2
  • 50
    • 33750615086 scopus 로고    scopus 로고
    • Rhodopsin-transducin coupling: Role of the Gα C-terminus in nucleotide exchange catalysis
    • Herrmann, R. et al. Rhodopsin-transducin coupling: role of the Gα C-terminus in nucleotide exchange catalysis. Vision Res. 46, 4582-4593 (2006).
    • (2006) Vision Res , vol.46 , pp. 4582-4593
    • Herrmann, R.1
  • 51
    • 0034048307 scopus 로고    scopus 로고
    • Assays for activation of opsin by all-trans-retinal
    • Sachs, K., Maretzki, D.& Hofmann, K. P. Assays for activation of opsin by all-trans-retinal. Methods Enzymol. 315, 238-251 (2000).
    • (2000) Methods Enzymol , vol.315 , pp. 238-251
    • Sachs, K.1    Maretzki, D.2    Hofmann, K.P.3
  • 52
    • 34249943432 scopus 로고    scopus 로고
    • Crystallization and crystal properties of squid rhodopsin
    • Murakami, M., Kitahara, R., Gotoh, T. & Kouyama, T. Crystallization and crystal properties of squid rhodopsin. Acta Crystallogr. F 63, 475-479 (2007).
    • (2007) Acta Crystallogr. F , vol.63 , pp. 475-479
    • Murakami, M.1    Kitahara, R.2    Gotoh, T.3    Kouyama, T.4
  • 53
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J. & Kim, S.-H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24, 409-411 (1991).
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 55
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 56
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 57
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-Building Tools for Molecular Graphics
    • Emsley, P. & Cowtan, K. Coot: Model-Building Tools for Molecular Graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 58
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 60
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K. & Thornton, J. M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793 (1994).
    • (1994) J. Mol. Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 61
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A. & Thornton, J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134 (1995).
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 62
    • 84945499796 scopus 로고    scopus 로고
    • DeLano, W. L. The PyMOL Molecular Graphics System. 〈http://www. pymol.org〉 (2002).
    • (2002)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.