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Volumn 377, Issue 5, 2008, Pages 1488-1497

Crystal Structure of Human Epidermal Kallikrein 7 (hK7) Synthesized Directly in its Native State in E. coli: Insights into the Atomic Basis of its Inhibition by LEKTI Domain 6 (LD6)

Author keywords

human tissue kallikreins; inhibition kinetics; LEKTI domain 6; serine proteases; X ray crystal structure

Indexed keywords

KALLIKREIN; KALLIKREIN 7; PROTEIN LEKTI DOMAIN 6; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 40849112916     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.089     Document Type: Article
Times cited : (15)

References (54)
  • 1
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: regulating cellular ecology
    • Werb Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91 (1997) 439-442
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 2
    • 0027948168 scopus 로고
    • Proteolytic action of thrombin is required for electrical activity-dependent synapse reduction
    • Liu Y., Fields R.D., Festoff B.W., and Nelson P.G. Proteolytic action of thrombin is required for electrical activity-dependent synapse reduction. Proc. Natl Acad. Sci. USA 91 (1994) 10300-10304
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10300-10304
    • Liu, Y.1    Fields, R.D.2    Festoff, B.W.3    Nelson, P.G.4
  • 3
    • 0018593041 scopus 로고
    • Kallikreins (kininogenases)-a group of serine proteases with bioregulatory actions
    • Schachter M. Kallikreins (kininogenases)-a group of serine proteases with bioregulatory actions. Pharmacol. Rev. 31 (1979) 1-17
    • (1979) Pharmacol. Rev. , vol.31 , pp. 1-17
    • Schachter, M.1
  • 4
    • 0034615555 scopus 로고    scopus 로고
    • Caspases - controlling intracellular signals by protease zymogen activation
    • Stennicke H.R., and Salvesen G.S. Caspases - controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta 1477 (2000) 299-306
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 299-306
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 6
    • 0035018273 scopus 로고    scopus 로고
    • The new human tissue kallikrein gene family: structure, function, and association to disease
    • Yousef G.M., and Diamandis E.P. The new human tissue kallikrein gene family: structure, function, and association to disease. Endocrinol. Rev. 22 (2001) 184-204
    • (2001) Endocrinol. Rev. , vol.22 , pp. 184-204
    • Yousef, G.M.1    Diamandis, E.P.2
  • 7
    • 0023888807 scopus 로고
    • Proteolytic degradation of desmosomes in plantar stratum corneum leads to cell dissociation in vitro
    • Egelrud T., Hofer P.A., and Lundstrom A. Proteolytic degradation of desmosomes in plantar stratum corneum leads to cell dissociation in vitro. Acta Derm. Venereol. 68 (1988) 93-97
    • (1988) Acta Derm. Venereol. , vol.68 , pp. 93-97
    • Egelrud, T.1    Hofer, P.A.2    Lundstrom, A.3
  • 8
    • 0029901712 scopus 로고    scopus 로고
    • Identification of a novel serine protease-like gene, the expression of which is down-regulated during breast cancer progression
    • Liu X.L., Wazer D.E., Watanabe K., and Band V. Identification of a novel serine protease-like gene, the expression of which is down-regulated during breast cancer progression. Cancer Res. 56 (1996) 3371-3379
    • (1996) Cancer Res. , vol.56 , pp. 3371-3379
    • Liu, X.L.1    Wazer, D.E.2    Watanabe, K.3    Band, V.4
  • 9
    • 0035870283 scopus 로고    scopus 로고
    • Cloning of a new member of the human kallikrein gene family, KLK14, which is down-regulated in different malignancies
    • Yousef G.M., Magklara A., Chang A., Jung K., Katsaros D., and Diamandis E.P. Cloning of a new member of the human kallikrein gene family, KLK14, which is down-regulated in different malignancies. Cancer Res. 61 (2001) 3425-3431
    • (2001) Cancer Res. , vol.61 , pp. 3425-3431
    • Yousef, G.M.1    Magklara, A.2    Chang, A.3    Jung, K.4    Katsaros, D.5    Diamandis, E.P.6
  • 10
    • 3543150203 scopus 로고    scopus 로고
    • Human tissue kallikreins: physiologic roles and applications in cancer
    • Borgono C.A., Michael I.P., and Diamandis E.P. Human tissue kallikreins: physiologic roles and applications in cancer. Mol. Cancer Res. 2 (2004) 257-280
    • (2004) Mol. Cancer Res. , vol.2 , pp. 257-280
    • Borgono, C.A.1    Michael, I.P.2    Diamandis, E.P.3
  • 11
    • 0026556434 scopus 로고
    • Bioregulation of kinins: kallikreins, kininogens, and kininases
    • Bhoola K.D., Figueroa C.D., and Worthy K. Bioregulation of kinins: kallikreins, kininogens, and kininases. Pharmacol. Rev. 44 (1992) 1-80
    • (1992) Pharmacol. Rev. , vol.44 , pp. 1-80
    • Bhoola, K.D.1    Figueroa, C.D.2    Worthy, K.3
  • 12
    • 0022357088 scopus 로고
    • A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein
    • Lilja H. A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein. J. Clin. Invest. 76 (1985) 1899-1903
    • (1985) J. Clin. Invest. , vol.76 , pp. 1899-1903
    • Lilja, H.1
  • 13
    • 8144222388 scopus 로고    scopus 로고
    • The emerging roles of human tissue kallikreins in cancer
    • Borgono C.A., and Diamandis E.P. The emerging roles of human tissue kallikreins in cancer. Nature Rev. Cancer 4 (2004) 876-890
    • (2004) Nature Rev. Cancer , vol.4 , pp. 876-890
    • Borgono, C.A.1    Diamandis, E.P.2
  • 14
    • 0027956112 scopus 로고
    • Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase
    • Hansson L., Stromqvist M., Backman A., Wallbrandt P., Carlstein A., and Egelrud T. Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase. J. Biol. Chem. 269 (1994) 19420-19426
    • (1994) J. Biol. Chem. , vol.269 , pp. 19420-19426
    • Hansson, L.1    Stromqvist, M.2    Backman, A.3    Wallbrandt, P.4    Carlstein, A.5    Egelrud, T.6
  • 15
    • 0034702897 scopus 로고    scopus 로고
    • The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family-genomic characterization, mapping, tissue expression and hormonal regulation
    • Yousef G.M., Scorilas A., Magklara A., Soosaipillai A., and Diamandis E.P. The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family-genomic characterization, mapping, tissue expression and hormonal regulation. Gene 254 (2000) 119-128
    • (2000) Gene , vol.254 , pp. 119-128
    • Yousef, G.M.1    Scorilas, A.2    Magklara, A.3    Soosaipillai, A.4    Diamandis, E.P.5
  • 16
    • 33947498991 scopus 로고    scopus 로고
    • A potential role for multiple tissue kallikrein serine proteases in epidermal desquamation
    • Borgono C.A., Michael I.P., Komatsu N., Jayakumar A., Kapadia R., Clayman G.L., et al. A potential role for multiple tissue kallikrein serine proteases in epidermal desquamation. J. Biol. Chem. 282 (2007) 3640-3652
    • (2007) J. Biol. Chem. , vol.282 , pp. 3640-3652
    • Borgono, C.A.1    Michael, I.P.2    Komatsu, N.3    Jayakumar, A.4    Kapadia, R.5    Clayman, G.L.6
  • 17
    • 2442428082 scopus 로고    scopus 로고
    • Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
    • Caubet C., Jonca N., Brattsand M., Guerrin M., Bernard D., Schmidt R., et al. Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J. Invest. Dermatol. 122 (2004) 1235-1244
    • (2004) J. Invest. Dermatol. , vol.122 , pp. 1235-1244
    • Caubet, C.1    Jonca, N.2    Brattsand, M.3    Guerrin, M.4    Bernard, D.5    Schmidt, R.6
  • 18
    • 0032934075 scopus 로고    scopus 로고
    • Stratum corneum chymotryptic enzyme in psoriasis
    • Ekholm E., and Egelrud T. Stratum corneum chymotryptic enzyme in psoriasis. Arch. Dermatol. Res. 291 (1999) 195-200
    • (1999) Arch. Dermatol. Res. , vol.291 , pp. 195-200
    • Ekholm, E.1    Egelrud, T.2
  • 19
    • 0033571558 scopus 로고    scopus 로고
    • The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells
    • Tanimoto H., Underwood L.J., Shigemasa K., Yan M., Yan S., Clarke J., et al. The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells. Cancer 86 (1999) 2074-2082
    • (1999) Cancer , vol.86 , pp. 2074-2082
    • Tanimoto, H.1    Underwood, L.J.2    Shigemasa, K.3    Yan, M.4    Yan, S.5    Clarke, J.6
  • 20
    • 34247597726 scopus 로고    scopus 로고
    • Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin
    • Johnson S.K., Ramani V.C., Hennings L., and Haun R.S. Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin. Cancer 109 (2007) 1811-1820
    • (2007) Cancer , vol.109 , pp. 1811-1820
    • Johnson, S.K.1    Ramani, V.C.2    Hennings, L.3    Haun, R.S.4
  • 21
    • 28844473475 scopus 로고    scopus 로고
    • hK5 and hK7, two serine proteinases abundant in human skin, are inhibited by LEKTI domain 6
    • Egelrud T., Brattsand M., Kreutzmann P., Walden M., Vitzithum K., Marx U.C., et al. hK5 and hK7, two serine proteinases abundant in human skin, are inhibited by LEKTI domain 6. Br. J. Dermatol. 153 (2005) 1200-1203
    • (2005) Br. J. Dermatol. , vol.153 , pp. 1200-1203
    • Egelrud, T.1    Brattsand, M.2    Kreutzmann, P.3    Walden, M.4    Vitzithum, K.5    Marx, U.C.6
  • 23
    • 0034120666 scopus 로고    scopus 로고
    • Mutations in SPINK5, encoding a serine protease inhibitor, cause Netherton syndrome
    • Chavanas S., Bodemer C., Rochat A., Hamel-Teillac D., Ali M., Irvine A.D., et al. Mutations in SPINK5, encoding a serine protease inhibitor, cause Netherton syndrome. Nature Genet. 25 (2000) 1141-1142
    • (2000) Nature Genet. , vol.25 , pp. 1141-1142
    • Chavanas, S.1    Bodemer, C.2    Rochat, A.3    Hamel-Teillac, D.4    Ali, M.5    Irvine, A.D.6
  • 25
    • 28244435723 scopus 로고    scopus 로고
    • Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI)
    • Schechter N.M., Choi E.J., Wang Z.M., Hanakawa Y., Stanley J.R., Kang Y., et al. Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI). Biol. Chem. 386 (2005) 1173-1184
    • (2005) Biol. Chem. , vol.386 , pp. 1173-1184
    • Schechter, N.M.1    Choi, E.J.2    Wang, Z.M.3    Hanakawa, Y.4    Stanley, J.R.5    Kang, Y.6
  • 26
    • 0031956299 scopus 로고    scopus 로고
    • Crystal structure of recombinant human tissue kallikrein at 2.0 Å resolution
    • Katz B.A., Liu B., Barnes M., and Springman E.B. Crystal structure of recombinant human tissue kallikrein at 2.0 Å resolution. Protein Sci. 7 (1998) 875-885
    • (1998) Protein Sci. , vol.7 , pp. 875-885
    • Katz, B.A.1    Liu, B.2    Barnes, M.3    Springman, E.B.4
  • 27
    • 33748644034 scopus 로고    scopus 로고
    • Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site
    • Debela M., Magdolen V., Grimminger V., Sommerhoff C., Messerschmidt A., Huber R., et al. Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. J. Mol. Biol. 362 (2006) 1094-1107
    • (2006) J. Mol. Biol. , vol.362 , pp. 1094-1107
    • Debela, M.1    Magdolen, V.2    Grimminger, V.3    Sommerhoff, C.4    Messerschmidt, A.5    Huber, R.6
  • 28
    • 0037025309 scopus 로고    scopus 로고
    • Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system
    • Bernett M.J., Blaber S.I., Scarisbrick I.A., Dhanarajan P., Thompson S.M., and Blaber M. Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system. J. Biol. Chem. 277 (2002) 24562-24570
    • (2002) J. Biol. Chem. , vol.277 , pp. 24562-24570
    • Bernett, M.J.1    Blaber, S.I.2    Scarisbrick, I.A.3    Dhanarajan, P.4    Thompson, S.M.5    Blaber, M.6
  • 29
    • 0037178833 scopus 로고    scopus 로고
    • The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family
    • Gomis-Ruth F.X., Bayes A., Sotiropoulou G., Pampalakis G., Tsetsenis T., Villegas V., et al. The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family. J. Biol. Chem. 277 (2002) 27273-27281
    • (2002) J. Biol. Chem. , vol.277 , pp. 27273-27281
    • Gomis-Ruth, F.X.1    Bayes, A.2    Sotiropoulou, G.3    Pampalakis, G.4    Tsetsenis, T.5    Villegas, V.6
  • 30
    • 34547630850 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family
    • Fernández I., Ständker L., Forssmann W., Giménez-Gallego G., and Romero A. Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family. Acta Crystallogr. F 63 (2007) 669-672
    • (2007) Acta Crystallogr. F , vol.63 , pp. 669-672
    • Fernández, I.1    Ständker, L.2    Forssmann, W.3    Giménez-Gallego, G.4    Romero, A.5
  • 32
    • 36048940448 scopus 로고    scopus 로고
    • Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7
    • Debela M., Hess P., Magdolen V., Schechter N.M., Steiner T., Huber R., et al. Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7. Proc. Natl Acad. Sci. USA 104 (2007) 16086-16091
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16086-16091
    • Debela, M.1    Hess, P.2    Magdolen, V.3    Schechter, N.M.4    Steiner, T.5    Huber, R.6
  • 34
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • Andrade M.A., Chacón P., Merelo J.J., and Morán F. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 35
    • 0029058938 scopus 로고
    • Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme
    • Skytt A., Stromqvist M., and Egelrud T. Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme. Biochem. Biophys. Res. Commun. 211 (1995) 586-589
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 586-589
    • Skytt, A.1    Stromqvist, M.2    Egelrud, T.3
  • 36
    • 1542719189 scopus 로고    scopus 로고
    • Recombinant production, purification and biochemical characterization of domain 6 of LEKTI: a temporary Kazal-type-related serine proteinase inhibitor
    • Kreutzmann P., Schulz A., Standker L., Forssmann W.G., and Magert H.J. Recombinant production, purification and biochemical characterization of domain 6 of LEKTI: a temporary Kazal-type-related serine proteinase inhibitor. J Chromatogr. B 803 (2004) 75-81
    • (2004) J Chromatogr. B , vol.803 , pp. 75-81
    • Kreutzmann, P.1    Schulz, A.2    Standker, L.3    Forssmann, W.G.4    Magert, H.J.5
  • 37
    • 0033548087 scopus 로고    scopus 로고
    • Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis
    • Kishi T., Kato M., Shimizu T., Kato K., Matsumoto K., Yoshida S., et al. Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis. J. Biol. Chem. 274 (1999) 4220-4224
    • (1999) J. Biol. Chem. , vol.274 , pp. 4220-4224
    • Kishi, T.1    Kato, M.2    Shimizu, T.3    Kato, K.4    Matsumoto, K.5    Yoshida, S.6
  • 38
    • 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
  • 40
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • Dasgupta S., Iyer G.H., Bryant S.H., Lawrence C.E., and Bell J.A. Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers. Proteins: Struct. Funct. Genet. 28 (1997) 494-514
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 494-514
    • Dasgupta, S.1    Iyer, G.H.2    Bryant, S.H.3    Lawrence, C.E.4    Bell, J.A.5
  • 41
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk A.M., and Fordham W.D. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258 (1996) 501-537
    • (1996) J. Mol. Biol. , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 42
    • 33748646005 scopus 로고    scopus 로고
    • Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences
    • Debela M., Magdolen V., Schechter N., Valachova M., Lottspeich F., Craik C.S., et al. Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences. J. Biol. Chem. 281 (2006) 25678-25688
    • (2006) J. Biol. Chem. , vol.281 , pp. 25678-25688
    • Debela, M.1    Magdolen, V.2    Schechter, N.3    Valachova, M.4    Lottspeich, F.5    Craik, C.S.6
  • 43
    • 0344642994 scopus 로고    scopus 로고
    • Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI
    • Lauber T., Schulz A., Schweimer K., Adermann K., and Marx U.C. Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI. J. Mol. Biol. 328 (2003) 205-219
    • (2003) J. Mol. Biol. , vol.328 , pp. 205-219
    • Lauber, T.1    Schulz, A.2    Schweimer, K.3    Adermann, K.4    Marx, U.C.5
  • 44
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668-W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 45
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. D 62 (2006) 48-57
    • (2006) Acta Crystallogr. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 46
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. Scaling and assessment of data quality. Acta Crystallogr. D 62 (2006) 72-82
    • (2006) Acta Crystallogr. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 47
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 48
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 49
    • 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
  • 50
    • 0032078747 scopus 로고    scopus 로고
    • A translation-function approach for heavy-atom location in macromolecular crystallography
    • Vagin A., and Teplyakov A. A translation-function approach for heavy-atom location in macromolecular crystallography. Acta Crystallogr. D 54 (1998) 400-402
    • (1998) Acta Crystallogr. D , vol.54 , pp. 400-402
    • Vagin, A.1    Teplyakov, A.2
  • 53
    • 0020491487 scopus 로고
    • Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 Å resolution. Structure solution, crystallographic refinement and preliminary structural interpretation
    • Bolognesi M., Gatti G., Menagatti E., Guarneri M., Marquart M., Papamokos E., and Huber R. Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 Å resolution. Structure solution, crystallographic refinement and preliminary structural interpretation. J. Mol. Biol. 162 (1982) 839-868
    • (1982) J. Mol. Biol. , vol.162 , pp. 839-868
    • Bolognesi, M.1    Gatti, G.2    Menagatti, E.3    Guarneri, M.4    Marquart, M.5    Papamokos, E.6    Huber, R.7


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