메뉴 건너뛰기




Volumn 388, Issue 3, 2009, Pages 520-540

Crystal Structures of the Histo-Aspartic Protease (HAP) from Plasmodium falciparum

Author keywords

aspartic proteases; crystal structure; inhibitor binding

Indexed keywords

APOENZYME; ASPARTIC ACID; ASPARTIC PROTEINASE; GLUTAMIC ACID; HISTIDINE; HISTOASPARTIC PROTEASE; KNI 1006; MONOMER; PEPSTATIN; PLASMEPSIN I; SERINE PROTEINASE; UNCLASSIFIED DRUG; ZINC;

EID: 64649106677     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.03.011     Document Type: Article
Times cited : (50)

References (58)
  • 1
    • 0037154180 scopus 로고    scopus 로고
    • Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine
    • Banerjee R., Liu J., Beatty W., Pelosof L., Klemba M., and Goldberg D.E. Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc. Natl Acad. Sci. USA 99 (2002) 990-995
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 2
    • 33747177314 scopus 로고    scopus 로고
    • Plasmepsins as potential targets for new antimalarial therapy
    • Ersmark K., Samuelsson B., and Hallberg A. Plasmepsins as potential targets for new antimalarial therapy. Med. Res. Rev. 26 (2006) 626-666
    • (2006) Med. Res. Rev. , vol.26 , pp. 626-666
    • Ersmark, K.1    Samuelsson, B.2    Hallberg, A.3
  • 3
    • 0032971605 scopus 로고    scopus 로고
    • A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum
    • Berry C., Humphreys M.J., Matharu P., Granger R., Horrocks P., Moon R.P., et al. A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum. FEBS Lett. 447 (1999) 149-154
    • (1999) FEBS Lett. , vol.447 , pp. 149-154
    • Berry, C.1    Humphreys, M.J.2    Matharu, P.3    Granger, R.4    Horrocks, P.5    Moon, R.P.6
  • 4
    • 2442476515 scopus 로고    scopus 로고
    • Is histoaspartic protease a serine protease with a pepsin-like fold?
    • Andreeva N., Bogdanovich P., Kashparov I., Popov M., and Stengach M. Is histoaspartic protease a serine protease with a pepsin-like fold?. Proteins 55 (2004) 705-710
    • (2004) Proteins , vol.55 , pp. 705-710
    • Andreeva, N.1    Bogdanovich, P.2    Kashparov, I.3    Popov, M.4    Stengach, M.5
  • 5
    • 8744303696 scopus 로고    scopus 로고
    • Computational prediction of structure, substrate binding mode, mechanism, and rate for a malaria protease with a novel type of active site
    • Bjelic S., and Aqvist J. Computational prediction of structure, substrate binding mode, mechanism, and rate for a malaria protease with a novel type of active site. Biochemistry 43 (2004) 14521-14528
    • (2004) Biochemistry , vol.43 , pp. 14521-14528
    • Bjelic, S.1    Aqvist, J.2
  • 6
    • 33747750905 scopus 로고    scopus 로고
    • Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum
    • Xiao H., Sinkovits A.F., Bryksa B.C., Ogawa M., and Yada R.Y. Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum. Protein Expression Purif. 49 (2006) 88-94
    • (2006) Protein Expression Purif. , vol.49 , pp. 88-94
    • Xiao, H.1    Sinkovits, A.F.2    Bryksa, B.C.3    Ogawa, M.4    Yada, R.Y.5
  • 7
    • 41549158249 scopus 로고    scopus 로고
    • The catalytic significance of the proposed active site residues in Plasmodium falciparum histoaspartic protease
    • Parr C.L., Tanaka T., Xiao H., and Yada R.Y. The catalytic significance of the proposed active site residues in Plasmodium falciparum histoaspartic protease. FEBS J. 275 (2008) 1698-1707
    • (2008) FEBS J. , vol.275 , pp. 1698-1707
    • Parr, C.L.1    Tanaka, T.2    Xiao, H.3    Yada, R.Y.4
  • 9
    • 0037780064 scopus 로고    scopus 로고
    • High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor
    • Nezami A., Kimura T., Hidaka K., Kiso A., Liu J., Kiso Y., et al. High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor. Biochemistry 42 (2003) 8459-8464
    • (2003) Biochemistry , vol.42 , pp. 8459-8464
    • Nezami, A.1    Kimura, T.2    Hidaka, K.3    Kiso, A.4    Liu, J.5    Kiso, Y.6
  • 11
    • 34247534257 scopus 로고    scopus 로고
    • Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?
    • Jaskolski M., Gilski M., Dauter Z., and Wlodawer A. Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?. Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 (2007) 611-620
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 611-620
    • Jaskolski, M.1    Gilski, M.2    Dauter, Z.3    Wlodawer, A.4
  • 12
    • 37349016530 scopus 로고    scopus 로고
    • Protein crystallography for non-crystallographers or how to get the best (but not more) from the published macromolecular structures
    • Wlodawer A., Minor W., Dauter Z., and Jaskolski M. Protein crystallography for non-crystallographers or how to get the best (but not more) from the published macromolecular structures. FEBS J. 275 (2008) 1-21
    • (2008) FEBS J. , vol.275 , pp. 1-21
    • Wlodawer, A.1    Minor, W.2    Dauter, Z.3    Jaskolski, M.4
  • 13
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn B.M. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 102 (2002) 4431-4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 14
    • 0041341883 scopus 로고    scopus 로고
    • Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides
    • Erskine P.T., Coates L., Mall S., Gill R.S., Wood S.P., Myles D.A., and Cooper J.B. Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides. Protein Sci. 12 (2003) 1741-1749
    • (2003) Protein Sci. , vol.12 , pp. 1741-1749
    • Erskine, P.T.1    Coates, L.2    Mall, S.3    Gill, R.S.4    Wood, S.P.5    Myles, D.A.6    Cooper, J.B.7
  • 15
    • 0037436389 scopus 로고    scopus 로고
    • Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum
    • Asojo O.A., Gulnik S.V., Afonina E., Yu B., Ellman J.A., Haque T.S., and Silva A.M. Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum. J. Mol. Biol. 327 (2003) 173-181
    • (2003) J. Mol. Biol. , vol.327 , pp. 173-181
    • Asojo, O.A.1    Gulnik, S.V.2    Afonina, E.3    Yu, B.4    Ellman, J.A.5    Haque, T.S.6    Silva, A.M.7
  • 16
  • 17
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions.
    • Cohen G.E. ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. J. Appl. Crystallogr. 30 (1997) 1160-1161
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 18
    • 0036900890 scopus 로고    scopus 로고
    • Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 Å in complex with the inhibitors rs367 and rs370
    • Asojo O.A., Afonina E., Gulnik S.V., Yu B., Erickson J.W., Randad R., et al. Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 Å in complex with the inhibitors rs367 and rs370. Acta Crystallogr., Sect. D: Biol. Crystallogr. 58 (2002) 2001-2008
    • (2002) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.58 , pp. 2001-2008
    • Asojo, O.A.1    Afonina, E.2    Gulnik, S.V.3    Yu, B.4    Erickson, J.W.5    Randad, R.6
  • 20
    • 0025276666 scopus 로고
    • Revised 2.3 Å structure of porcine pepsin: evidence for a flexible subdomain
    • Abad-Zapatero C., Rydel T.J., and Erickson J. Revised 2.3 Å structure of porcine pepsin: evidence for a flexible subdomain. Proteins 8 (1990) 62-81
    • (1990) Proteins , vol.8 , pp. 62-81
    • Abad-Zapatero, C.1    Rydel, T.J.2    Erickson, J.3
  • 21
    • 0029366979 scopus 로고
    • Comparison of three-dimensional structures of flexible protein molecules
    • Andreeva N.S., and Pechik I.V. Comparison of three-dimensional structures of flexible protein molecules. Mol. Biol. (Moscow) 29 (1995) 1102-1113
    • (1995) Mol. Biol. (Moscow) , vol.29 , pp. 1102-1113
    • Andreeva, N.S.1    Pechik, I.V.2
  • 22
    • 0025374191 scopus 로고
    • The three-dimensional structure of recombinant bovine chymosin at 2.3 Å resolution
    • Gilliland G.L., Winborne E.L., Nachman J., and Wlodawer A. The three-dimensional structure of recombinant bovine chymosin at 2.3 Å resolution. Proteins 8 (1990) 82-101
    • (1990) Proteins , vol.8 , pp. 82-101
    • Gilliland, G.L.1    Winborne, E.L.2    Nachman, J.3    Wlodawer, A.4
  • 23
    • 0025214572 scopus 로고
    • On the role of peripheral interactions in specificity of chymosin
    • Safro M.G., and Andreeva N.S. On the role of peripheral interactions in specificity of chymosin. Biochem. Int. 20 (1990) 555-561
    • (1990) Biochem. Int. , vol.20 , pp. 555-561
    • Safro, M.G.1    Andreeva, N.S.2
  • 24
    • 0030054003 scopus 로고    scopus 로고
    • Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of kappa-casein
    • Gustchina E., Rumsh L., Ginodman L., Majer P., and Andreeva N. Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of kappa-casein. FEBS Lett. 379 (1996) 60-62
    • (1996) FEBS Lett. , vol.379 , pp. 60-62
    • Gustchina, E.1    Rumsh, L.2    Ginodman, L.3    Majer, P.4    Andreeva, N.5
  • 25
    • 14844302643 scopus 로고    scopus 로고
    • Distal substrate interactions enhance plasmepsin activity
    • Istvan E.S., and Goldberg D.E. Distal substrate interactions enhance plasmepsin activity. J. Biol. Chem. 280 (2005) 6890-6896
    • (2005) J. Biol. Chem. , vol.280 , pp. 6890-6896
    • Istvan, E.S.1    Goldberg, D.E.2
  • 27
    • 11144237489 scopus 로고    scopus 로고
    • Genetic disruption of the Plasmodium falciparum digestive vacuole plasmepsins demonstrates their functional redundancy
    • Omara-Opyene A.L., Moura P.A., Sulsona C.R., Bonilla J.A., Yowell C.A., Fujioka H., et al. Genetic disruption of the Plasmodium falciparum digestive vacuole plasmepsins demonstrates their functional redundancy. J. Biol. Chem. 279 (2004) 54088-54096
    • (2004) J. Biol. Chem. , vol.279 , pp. 54088-54096
    • Omara-Opyene, A.L.1    Moura, P.A.2    Sulsona, C.R.3    Bonilla, J.A.4    Yowell, C.A.5    Fujioka, H.6
  • 28
    • 0026345730 scopus 로고
    • KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic
    • Mimoto T., Imai J., Tanaka S., Hattori N., Kisanuki S., Akaji K., and Kiso Y. KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic. Chem. Pharm. Bull. (Tokyo) 39 (1991) 3088-3090
    • (1991) Chem. Pharm. Bull. (Tokyo) , vol.39 , pp. 3088-3090
    • Mimoto, T.1    Imai, J.2    Tanaka, S.3    Hattori, N.4    Kisanuki, S.5    Akaji, K.6    Kiso, Y.7
  • 29
    • 0025943905 scopus 로고
    • Rational design and synthesis of a novel class of active site-targeted HIV protease inhibitors containing a hydroxymethylcarbonyl isostere. Use of phenylnorstatine or allophenylnorstatine as a transition-state mimic
    • Mimoto T., Imai J., Tanaka S., Hattori N., Takahashi O., Kisanuki S., et al. Rational design and synthesis of a novel class of active site-targeted HIV protease inhibitors containing a hydroxymethylcarbonyl isostere. Use of phenylnorstatine or allophenylnorstatine as a transition-state mimic. Chem. Pharm. Bull. (Tokyo) 39 (1991) 2465-2467
    • (1991) Chem. Pharm. Bull. (Tokyo) , vol.39 , pp. 2465-2467
    • Mimoto, T.1    Imai, J.2    Tanaka, S.3    Hattori, N.4    Takahashi, O.5    Kisanuki, S.6
  • 30
    • 0029943637 scopus 로고    scopus 로고
    • Design and synthesis of substrate-based peptidomimetic human immunodeficiency virus protease inhibitors containing the hydroxymethylcarbonyl isostere
    • Kiso Y. Design and synthesis of substrate-based peptidomimetic human immunodeficiency virus protease inhibitors containing the hydroxymethylcarbonyl isostere. Biopolymers 40 (1996) 235-244
    • (1996) Biopolymers , vol.40 , pp. 235-244
    • Kiso, Y.1
  • 31
    • 7044254904 scopus 로고    scopus 로고
    • Identification of peptidomimetic HTLV-I protease inhibitors containing hydroxymethylcarbonyl (HMC) isostere as the transition-state mimic
    • Maegawa H., Kimura T., Arii Y., Matsui Y., Kasai S., Hayashi Y., and Kiso Y. Identification of peptidomimetic HTLV-I protease inhibitors containing hydroxymethylcarbonyl (HMC) isostere as the transition-state mimic. Bioorg. Med. Chem. Lett. 14 (2004) 5925-5929
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 5925-5929
    • Maegawa, H.1    Kimura, T.2    Arii, Y.3    Matsui, Y.4    Kasai, S.5    Hayashi, Y.6    Kiso, Y.7
  • 32
    • 10044264132 scopus 로고    scopus 로고
    • Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases
    • Abdel-Rahman H.M., Kimura T., Hidaka K., Kiso A., Nezami A., Freire E., et al. Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases. Biol. Chem. 385 (2004) 1035-1039
    • (2004) Biol. Chem. , vol.385 , pp. 1035-1039
    • Abdel-Rahman, H.M.1    Kimura, T.2    Hidaka, K.3    Kiso, A.4    Nezami, A.5    Freire, E.6
  • 33
    • 34249289725 scopus 로고    scopus 로고
    • Chipping at large, potent human T-cell leukemia virus type 1 protease inhibitors to uncover smaller, equipotent inhibitors
    • Kimura T., Nguyen J.T., Maegawa H., Nishiyama K., Arii Y., Matsui Y., et al. Chipping at large, potent human T-cell leukemia virus type 1 protease inhibitors to uncover smaller, equipotent inhibitors. Bioorg. Med. Chem. Lett. 17 (2007) 3276-3280
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 3276-3280
    • Kimura, T.1    Nguyen, J.T.2    Maegawa, H.3    Nishiyama, K.4    Arii, Y.5    Matsui, Y.6
  • 34
    • 37548998994 scopus 로고    scopus 로고
    • Truncation and non-natural amino acid substitution studies on HTLV-I protease hexapeptidic inhibitors
    • Nguyen J.T., Zhang M., Kumada H.O., Itami A., Nishiyama K., Kimura T., et al. Truncation and non-natural amino acid substitution studies on HTLV-I protease hexapeptidic inhibitors. Bioorg. Med. Chem. Lett. 18 (2008) 366-370
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 366-370
    • Nguyen, J.T.1    Zhang, M.2    Kumada, H.O.3    Itami, A.4    Nishiyama, K.5    Kimura, T.6
  • 36
    • 43749120718 scopus 로고    scopus 로고
    • Synthesis and activity of tetrapeptidic HTLV-I protease inhibitors possessing different P3-cap moieties
    • Zhang M., Nguyen J.T., Kumada H.O., Kimura T., Cheng M., Hayashi Y., and Kiso Y. Synthesis and activity of tetrapeptidic HTLV-I protease inhibitors possessing different P3-cap moieties. Bioorg. Med. Chem. 16 (2008) 5795-5802
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 5795-5802
    • Zhang, M.1    Nguyen, J.T.2    Kumada, H.O.3    Kimura, T.4    Cheng, M.5    Hayashi, Y.6    Kiso, Y.7
  • 37
    • 55749114914 scopus 로고    scopus 로고
    • Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin
    • Hidaka K., Kimura T., Ruben A.J., Uemura T., Kamiya M., Kiso A., et al. Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin. Bioorg. Med. Chem. 16 (2008) 10049-10060
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 10049-10060
    • Hidaka, K.1    Kimura, T.2    Ruben, A.J.3    Uemura, T.4    Kamiya, M.5    Kiso, A.6
  • 38
    • 0025108755 scopus 로고
    • Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0 Å resolution
    • Fitzgerald P.M.D., McKeever B.M., VanMiddlesworth J.F., Springer J.P., Heimbach J.C., Leu C.T., et al. Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0 Å resolution. J. Biol. Chem. 265 (1990) 14209-14219
    • (1990) J. Biol. Chem. , vol.265 , pp. 14209-14219
    • Fitzgerald, P.M.D.1    McKeever, B.M.2    VanMiddlesworth, J.F.3    Springer, J.P.4    Heimbach, J.C.5    Leu, C.T.6
  • 39
    • 0033102135 scopus 로고    scopus 로고
    • Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases?
    • Oefner C., Binggeli A., Breu V., Bur D., Clozel J.P., D'Arcy A., et al. Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases?. Chem. Biol. 6 (1999) 127-131
    • (1999) Chem. Biol. , vol.6 , pp. 127-131
    • Oefner, C.1    Binggeli, A.2    Breu, V.3    Bur, D.4    Clozel, J.P.5    D'Arcy, A.6
  • 41
    • 33746276423 scopus 로고    scopus 로고
    • Starving the malaria parasite: inhibitors active against the aspartic proteases plasmepsins I, II, and IV
    • Hof F., Schutz A., Fah C., Meyer S., Bur D., Liu J., et al. Starving the malaria parasite: inhibitors active against the aspartic proteases plasmepsins I, II, and IV. Angew. Chem., Int. Ed. Engl. 45 (2006) 2138-2141
    • (2006) Angew. Chem., Int. Ed. Engl. , vol.45 , pp. 2138-2141
    • Hof, F.1    Schutz, A.2    Fah, C.3    Meyer, S.4    Bur, D.5    Liu, J.6
  • 43
    • 0021767550 scopus 로고
    • The active site of aspartic proteinases
    • Pearl L., and Blundell T. The active site of aspartic proteinases. FEBS Lett. 174 (1984) 96-101
    • (1984) FEBS Lett. , vol.174 , pp. 96-101
    • Pearl, L.1    Blundell, T.2
  • 44
    • 0035188306 scopus 로고    scopus 로고
    • Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes
    • Andreeva N.S., and Rumsh L.D. Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes. Protein Sci. 10 (2001) 2439-2450
    • (2001) Protein Sci. , vol.10 , pp. 2439-2450
    • Andreeva, N.S.1    Rumsh, L.D.2
  • 45
    • 0024412506 scopus 로고
    • Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease
    • Wlodawer A., Miller M., Jaskólski M., Sathyanarayana B.K., Baldwin E., Weber I.T., et al. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 245 (1989) 616-621
    • (1989) Science , vol.245 , pp. 616-621
    • Wlodawer, A.1    Miller, M.2    Jaskólski, M.3    Sathyanarayana, B.K.4    Baldwin, E.5    Weber, I.T.6
  • 46
    • 0024492495 scopus 로고
    • Crystal structure of a retroviral protease proves relationship to aspartic protease family
    • Miller M., Jaskólski M., Rao J.K.M., Leis J., and Wlodawer A. Crystal structure of a retroviral protease proves relationship to aspartic protease family. Nature 337 (1989) 576-579
    • (1989) Nature , vol.337 , pp. 576-579
    • Miller, M.1    Jaskólski, M.2    Rao, J.K.M.3    Leis, J.4    Wlodawer, A.5
  • 47
    • 0034881189 scopus 로고    scopus 로고
    • Structure of the Bacillus subtilis d-aminopeptidase DppA reveals a novel self-compartmentalizing protease
    • Remaut H., Bompard-Gilles C., Goffin C., Frere J.M., and Van Beeumen J. Structure of the Bacillus subtilis d-aminopeptidase DppA reveals a novel self-compartmentalizing protease. Nat. Struct. Biol. 8 (2001) 674-678
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 674-678
    • Remaut, H.1    Bompard-Gilles, C.2    Goffin, C.3    Frere, J.M.4    Van Beeumen, J.5
  • 49
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 52
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 53
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr., Sect. D: Biol. Crystallogr. 57 (2001) 1373-1382
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 54
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 57
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2256-2268
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.