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Volumn 155, Issue 3, 2006, Pages 445-457

The transthyretin-related protein: Structural investigation of a novel protein family

Author keywords

Crystal structure; Escherichia coli; Transthyretin; Transthyretin related protein; TRP

Indexed keywords

BROMIDE; PREALBUMIN; TRANSTHYRETIN RELATED PROTEIN; UNCLASSIFIED DRUG; ZINC;

EID: 33748788511     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.04.002     Document Type: Article
Times cited : (34)

References (57)
  • 1
    • 1542320018 scopus 로고    scopus 로고
    • Sulfite and base for the treatment of familial amyloidotic polyneuropathy: two additive approaches to stabilize the conformation of human amyloidogenic transthyretin
    • Altland K., Winter P., Saraiva M.J., and Suhr O. Sulfite and base for the treatment of familial amyloidotic polyneuropathy: two additive approaches to stabilize the conformation of human amyloidogenic transthyretin. Neurogenetics 5 (2004) 61-67
    • (2004) Neurogenetics , vol.5 , pp. 61-67
    • Altland, K.1    Winter, P.2    Saraiva, M.J.3    Suhr, O.4
  • 2
    • 0032994562 scopus 로고    scopus 로고
    • Electrically neutral microheterogeneity of human plasma transthyretin (prealbumin) detected by isoelectric focusing in urea gradients
    • Altland K., Winter P., and Sauerborn M.K. Electrically neutral microheterogeneity of human plasma transthyretin (prealbumin) detected by isoelectric focusing in urea gradients. Electrophoresis 20 (1999) 1349-1364
    • (1999) Electrophoresis , vol.20 , pp. 1349-1364
    • Altland, K.1    Winter, P.2    Sauerborn, M.K.3
  • 5
    • 0017824077 scopus 로고
    • Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A
    • Blake C.C., Geisow M.J., Oatley S.J., Rérat B., and Rérat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J. Mol. Biol. 121 (1978) 339-356
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rérat, B.4    Rérat, C.5
  • 6
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 8
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, N., 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, pp. 760-763.
  • 9
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa P.P., Figueira A.S., and Bravo F.R. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc. Natl. Acad. Sci. USA 75 (1978) 4499-4503
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4499-4503
    • Costa, P.P.1    Figueira, A.S.2    Bravo, F.R.3
  • 10
    • 0035865504 scopus 로고    scopus 로고
    • Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-d-thioglucoside
    • Czjzek M., Cicek M., Zamboni V., Burmeister W.P., Bevan D.R., Henrissat B., and Esen A. Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-d-thioglucoside. Biochem. J. 354 (2001) 37-46
    • (2001) Biochem. J. , vol.354 , pp. 37-46
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Burmeister, W.P.4    Bevan, D.R.5    Henrissat, B.6    Esen, A.7
  • 13
    • 2942741033 scopus 로고    scopus 로고
    • High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine
    • Eneqvist T., Lundberg E., Karlsson A., Huang S., Santos C.R., Power D.M., and Sauer-Eriksson A.E. High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine. J. Biol. Chem. 279 (2004) 26411-26416
    • (2004) J. Biol. Chem. , vol.279 , pp. 26411-26416
    • Eneqvist, T.1    Lundberg, E.2    Karlsson, A.3    Huang, S.4    Santos, C.R.5    Power, D.M.6    Sauer-Eriksson, A.E.7
  • 15
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., and Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47 (1991) 392-400
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 17
    • 0034799733 scopus 로고    scopus 로고
    • Transthyretin: a review from a structural perspective
    • Hamilton J.A., and Benson M.D. Transthyretin: a review from a structural perspective. Cell. Mol. Life Sci. 58 (2001) 1491-1521
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1491-1521
    • Hamilton, J.A.1    Benson, M.D.2
  • 18
    • 0027476367 scopus 로고
    • The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7-Å resolution
    • Hamilton J.A., Steinrauf L.K., Braden B.C., Liepnieks J., Benson M.D., Holmgren G., Sandgren O., and Steen L. The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7-Å resolution. J. Biol. Chem. 268 (1993) 2416-2424
    • (1993) J. Biol. Chem. , vol.268 , pp. 2416-2424
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Liepnieks, J.4    Benson, M.D.5    Holmgren, G.6    Sandgren, O.7    Steen, L.8
  • 19
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding M.M. Geometry of metal-ligand interactions in proteins. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 401-411
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 20
  • 21
  • 22
    • 21644435242 scopus 로고    scopus 로고
    • The effect of iodide and chloride on transthyretin structure and stability
    • Hornberg A., Hultdin U.W., Olofsson A., and Sauer-Eriksson A.E. The effect of iodide and chloride on transthyretin structure and stability. Biochemistry 44 (2005) 9290-9299
    • (2005) Biochemistry , vol.44 , pp. 9290-9299
    • Hornberg, A.1    Hultdin, U.W.2    Olofsson, A.3    Sauer-Eriksson, A.E.4
  • 23
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 24
    • 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. Cryst. 26 (1993) 795-800
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 25
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 26
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8 (1998) 101-106
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 27
    • 0030023632 scopus 로고    scopus 로고
    • Simple detection of abnormal serum transthyretin from patients with familial amyloidotic polyneuropathy by high-performance liquid chromatography/electrospray ionization mass spectrometry using material precipitated with specific antiserum
    • Kishikawa M., Nakanishi T., Miyazaki A., Shimizu A., Nakazato M., Kangawa K., and Matsuo H. Simple detection of abnormal serum transthyretin from patients with familial amyloidotic polyneuropathy by high-performance liquid chromatography/electrospray ionization mass spectrometry using material precipitated with specific antiserum. J. Mass Spectrom. 31 (1996) 112-114
    • (1996) J. Mass Spectrom. , vol.31 , pp. 112-114
    • Kishikawa, M.1    Nakanishi, T.2    Miyazaki, A.3    Shimizu, A.4    Nakazato, M.5    Kangawa, K.6    Matsuo, H.7
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 24044525647 scopus 로고    scopus 로고
    • Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction
    • Lee Y., Lee do H., Kho C.W., Lee A.Y., Jang M., Cho S., Lee C.H., Lee J.S., Myung P.K., Park B.C., and Park S.G. Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett. 579 (2005) 4769-4774
    • (2005) FEBS Lett. , vol.579 , pp. 4769-4774
    • Lee, Y.1    Lee do, H.2    Kho, C.W.3    Lee, A.Y.4    Jang, M.5    Cho, S.6    Lee, C.H.7    Lee, J.S.8    Myung, P.K.9    Park, B.C.10    Park, S.G.11
  • 30
    • 23944481361 scopus 로고    scopus 로고
    • Brassinosteroid signaling: from receptor kinases to transcription factors
    • Li J. Brassinosteroid signaling: from receptor kinases to transcription factors. Curr. Opin. Plant Biol. 8 (2005) 526-531
    • (2005) Curr. Opin. Plant Biol. , vol.8 , pp. 526-531
    • Li, J.1
  • 31
    • 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
  • 32
    • 4544236639 scopus 로고    scopus 로고
    • The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1
    • Nam K.H., and Li J. The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1. Plant Cell 16 (2004) 2406-2417
    • (2004) Plant Cell , vol.16 , pp. 2406-2417
    • Nam, K.H.1    Li, J.2
  • 33
    • 33748795427 scopus 로고    scopus 로고
    • Olofsson, A., Ippel, J.H., Wijmenga, S.S., Lundgren, E., Ohman, A., 2003. Probing solvent accessibility of transthyretin-amyloid by solution NMR spectroscopy. J. Biol. Chem.
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0036910380 scopus 로고    scopus 로고
    • Transthyretin as a thyroid hormone carrier: function revisited
    • Palha J.A. Transthyretin as a thyroid hormone carrier: function revisited. Clin. Chem. Lab. Med. 40 (2002) 1292-1300
    • (2002) Clin. Chem. Lab. Med. , vol.40 , pp. 1292-1300
    • Palha, J.A.1
  • 38
    • 33646580070 scopus 로고    scopus 로고
    • Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes
    • Ramazzina I., Folli C., Secchi A., Berni R., and Percudani R. Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat. Chem. Biol. 2 (2006) 144-148
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 144-148
    • Ramazzina, I.1    Folli, C.2    Secchi, A.3    Berni, R.4    Percudani, R.5
  • 39
    • 0036914860 scopus 로고    scopus 로고
    • Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism
    • Raychaudhuri A., and Tipton P.A. Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism. Plant Physiol. 130 (2002) 2061-2068
    • (2002) Plant Physiol. , vol.130 , pp. 2061-2068
    • Raychaudhuri, A.1    Tipton, P.A.2
  • 40
    • 0037646897 scopus 로고    scopus 로고
    • A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase
    • Raychaudhuri A., and Tipton P.A. A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase. Biochemistry 42 (2003) 6848-6852
    • (2003) Biochemistry , vol.42 , pp. 6848-6852
    • Raychaudhuri, A.1    Tipton, P.A.2
  • 41
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva M.J. Transthyretin mutations in health and disease. Hum. Mutat. 5 (1995) 191-196
    • (1995) Hum. Mutat. , vol.5 , pp. 191-196
    • Saraiva, M.J.1
  • 42
    • 0020924805 scopus 로고
    • Presence of an abnormal transthyretin (prealbumin) in Portuguese patients with familial amyloidotic polyneuropathy
    • Saraiva M.J., Costa P.P., Birken S., and Goodman D.S. Presence of an abnormal transthyretin (prealbumin) in Portuguese patients with familial amyloidotic polyneuropathy. Trans. Assoc. Am. Phys. 96 (1983) 261-270
    • (1983) Trans. Assoc. Am. Phys. , vol.96 , pp. 261-270
    • Saraiva, M.J.1    Costa, P.P.2    Birken, S.3    Goodman, D.S.4
  • 43
    • 0003081534 scopus 로고    scopus 로고
    • A simple method for making reproducible fibre loops for protein cryocrystallography
    • Sauer U.H., and Ceska T.A. A simple method for making reproducible fibre loops for protein cryocrystallography. J. Appl. Crystallogr. 30 (1997) 71-72
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 71-72
    • Sauer, U.H.1    Ceska, T.A.2
  • 44
    • 0001841380 scopus 로고
    • On the rigid-body motion of molecules in crystals
    • Schomaker V., and Trueblood K.N. On the rigid-body motion of molecules in crystals. Acta Crystallogr. B 24 (1968) 63-76
    • (1968) Acta Crystallogr. B , vol.24 , pp. 63-76
    • Schomaker, V.1    Trueblood, K.N.2
  • 45
    • 0035031537 scopus 로고    scopus 로고
    • Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator
    • Schultz A.C., Nygaard P., and Saxild H.H. Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J. Bacteriol. 183 (2001) 3293-3302
    • (2001) J. Bacteriol. , vol.183 , pp. 3293-3302
    • Schultz, A.C.1    Nygaard, P.2    Saxild, H.H.3
  • 46
    • 0032544408 scopus 로고    scopus 로고
    • The crystal structure of amyloidogenic Leu55 → Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
    • Sebastião M.P., Saraiva M.J., and Damas A.M. The crystal structure of amyloidogenic Leu55 → Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils. J. Biol. Chem. 273 (1998) 24715-24722
    • (1998) J. Biol. Chem. , vol.273 , pp. 24715-24722
    • Sebastião, M.P.1    Saraiva, M.J.2    Damas, A.M.3
  • 47
    • 0035822703 scopus 로고    scopus 로고
    • Identification of a subunit interface in transthyretin amyloid fibrils: evidence for self-assembly from oligomeric building blocks
    • Serag A.A., Altenbach C., Gingery M., Hubbell W.L., and Yeates T.O. Identification of a subunit interface in transthyretin amyloid fibrils: evidence for self-assembly from oligomeric building blocks. Biochemistry 40 (2001) 9089-9096
    • (2001) Biochemistry , vol.40 , pp. 9089-9096
    • Serag, A.A.1    Altenbach, C.2    Gingery, M.3    Hubbell, W.L.4    Yeates, T.O.5
  • 48
    • 1842589542 scopus 로고    scopus 로고
    • The "edge strand" hypothesis: Prediction and test of a mutational "hot-spot" on the transthyretin molecule associated with FAP amyloidogenesis
    • Serpell L.C., Goldsteins G., Dacklin I., Lundgren E., and Blake C.C.F. The "edge strand" hypothesis: Prediction and test of a mutational "hot-spot" on the transthyretin molecule associated with FAP amyloidogenesis. Amyloid: Int. J. Exp. Clin. Invest. 3 (1996) 75-85
    • (1996) Amyloid: Int. J. Exp. Clin. Invest. , vol.3 , pp. 75-85
    • Serpell, L.C.1    Goldsteins, G.2    Dacklin, I.3    Lundgren, E.4    Blake, C.C.F.5
  • 53
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D. Biol. Crystallogr. 57 (2001) 122-133
    • (2001) Acta Crystallogr. D. Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 54
    • 0031297816 scopus 로고    scopus 로고
    • Crystal structure of rat transthyretin at 2.5 Å resolution: first report on a unique tetrameric structure
    • Wojtczak A. Crystal structure of rat transthyretin at 2.5 Å resolution: first report on a unique tetrameric structure. Acta Biochim. Pol. 44 (1997) 505-517
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 505-517
    • Wojtczak, A.1
  • 55
    • 0030484635 scopus 로고    scopus 로고
    • Structures of human transthyretin complexed with thyroxine at 2.0 Å resolution and 3′,5′-dinitro-N-acetyl-l-thyronine at 2.2 Å resolution
    • Wojtczak A., Cody V., Luft J.R., and Pangborn W. Structures of human transthyretin complexed with thyroxine at 2.0 Å resolution and 3′,5′-dinitro-N-acetyl-l-thyronine at 2.2 Å resolution. Acta Crystallogr. D 52 (1996) 758-765
    • (1996) Acta Crystallogr. D , vol.52 , pp. 758-765
    • Wojtczak, A.1    Cody, V.2    Luft, J.R.3    Pangborn, W.4
  • 56
    • 0042848710 scopus 로고    scopus 로고
    • Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions
    • Zhang Q., and Kelly J.W. Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions. Biochemistry 42 (2003) 8756-8761
    • (2003) Biochemistry , vol.42 , pp. 8756-8761
    • Zhang, Q.1    Kelly, J.W.2
  • 57
    • 21744460057 scopus 로고    scopus 로고
    • Cys-10 mixed disulfide modifications exacerbate transthyretin familial variant amyloidogenicity: a likely explanation for variable clinical expression of amyloidosis and the lack of pathology in c10s/v30m transgenic mice?
    • Zhang Q., and Kelly J.W. Cys-10 mixed disulfide modifications exacerbate transthyretin familial variant amyloidogenicity: a likely explanation for variable clinical expression of amyloidosis and the lack of pathology in c10s/v30m transgenic mice?. Biochemistry 44 (2005) 9079-9085
    • (2005) Biochemistry , vol.44 , pp. 9079-9085
    • Zhang, Q.1    Kelly, J.W.2


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