메뉴 건너뛰기




Volumn 48, Issue 4, 2001, Pages 867-875

Structural basis of negative cooperativity in transthyretin

Author keywords

Negative cooperativity; Transthyretin

Indexed keywords

LIGAND; PREALBUMIN;

EID: 0035755698     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2001_3852     Document Type: Article
Times cited : (45)

References (27)
  • 1
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly, J.W. (1997) Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases. Structure 5, 595-600.
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 2
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation
    • Kelly, J.W. & Lansbury, P.T.J. (1994) A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation. Amyloid 1, 186-205.
    • (1994) Amyloid , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury, P.T.J.2
  • 4
    • 0017754889 scopus 로고
    • Protein-DNA and protein-hormone interactions in prealbumin: A model of the thyroid hormone nuclear receptor?
    • Blake, C.C.F & Oatley, S.J. (1977) Protein-DNA and protein-hormone interactions in prealbumin: A model of the thyroid hormone nuclear receptor? Nature 268, 115-129.
    • (1977) Nature , vol.268 , pp. 115-129
    • Blake, C.C.F.1    Oatley, S.J.2
  • 5
    • 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. & Pangborn, W. (1996) 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. D52, 758-765.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 758-765
    • Wojtczak, A.1    Cody, V.2    Luft, J.R.3    Pangborn, W.4
  • 6
    • 0026584392 scopus 로고
    • Mechanism of molecular recognition: Structural aspects of 3,3′-diiodo-L-thyronine binding to human serum transthyretin
    • Wojtczak, A., Luft, J. R. & Cody, V. (1992) Mechanism of molecular recognition: Structural aspects of 3,3′-diiodo-L-thyronine binding to human serum transthyretin. J. Biol. Chem. 267, 353-357.
    • (1992) J. Biol. Chem. , vol.267 , pp. 353-357
    • Wojtczak, A.1    Luft, J.R.2    Cody, V.3
  • 7
    • 0027499933 scopus 로고
    • Structural aspects of inotropic bipyridine binding: Crystal structure determination to 1.9 Å of the human serum transthyretin-milrinone complex
    • Wojtczak, A., Luft, J.R. & Cody, V. (1993) Structural aspects of inotropic bipyridine binding: Crystal structure determination to 1.9 Å of the human serum transthyretin-milrinone complex. J. Biol. Chem. 268, 6202-6206.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6202-6206
    • Wojtczak, A.1    Luft, J.R.2    Cody, V.3
  • 8
    • 0026723625 scopus 로고
    • Crystal structure determination at 2.3-Å resolution of human transthyretin-3′,5′-dibromo-2′,4,4′,6-tetrahydroxyaurone complex
    • Ciszak, E., Luft, J. & Cody, V. (1992) Crystal structure determination at 2.3-Å resolution of human transthyretin-3′,5′-dibromo-2′,4,4′,6-tetrahydroxyaurone complex. Proc. Natl. Acad. Sci. U.S.A. 89, 6644-6648.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6644-6648
    • Ciszak, E.1    Luft, J.2    Cody, V.3
  • 9
    • 0001769272 scopus 로고
    • Differences in inhibitor and substrate binding in transthyretin crystal complexes
    • (Gordon, A., Gross, J. & Hennemann, G., eds.) Balkema, Rotterdam
    • Cody, V., Wojtczak, A., Ciszak, E. & Luft, J. (1991) Differences in inhibitor and substrate binding in transthyretin crystal complexes; in Progress in Thyroid Research (Gordon, A., Gross, J. & Hennemann, G., eds.) pp. 793-796, Balkema, Rotterdam.
    • (1991) Progress in Thyroid Research , pp. 793-796
    • Cody, V.1    Wojtczak, A.2    Ciszak, E.3    Luft, J.4
  • 10
    • 0027476367 scopus 로고
    • The X-Ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val30Met variant to 1.7 Å resolution
    • Hamilton, J.A., Steinrauf, L.K., Braden, B.C., Liepniks, J., Benson, M.D., Holmgren, G., Sandgren, O. & Steen, L. (1993) The X-Ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val30Met variant to 1.7 Å resolution. J. Biol. Chem. 268, 2416-2424.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2416-2424
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Liepniks, J.4    Benson, M.D.5    Holmgren, G.6    Sandgren, O.7    Steen, L.8
  • 14
    • 0034703380 scopus 로고    scopus 로고
    • A comparative analysis of 23 structures of the amyloidogenic protein transthyretin
    • Hornberg, A., Eneqvist, T., Olofsson, A., Lundgren, E. & Sauer-Eriksson, A.E. (2000) A comparative analysis of 23 structures of the amyloidogenic protein transthyretin. J. Mol. Biol. 302, 649-669.
    • (2000) J. Mol. Biol. , vol.302 , pp. 649-669
    • Hornberg, A.1    Eneqvist, T.2    Olofsson, A.3    Lundgren, E.4    Sauer-Eriksson, A.E.5
  • 15
    • 0034934691 scopus 로고    scopus 로고
    • Structure of a new polymorphic monoclinic form of human transthyretin at 3 Å resolution reveals a mixed complex between unliganded and T4-bound tetramers of TTR
    • Wojtczak, A., Neumann, P. & Cody, V. (2001) Structure of a new polymorphic monoclinic form of human transthyretin at 3 Å resolution reveals a mixed complex between unliganded and T4-bound tetramers of TTR. Acta Crystallogr. D57, 957-967
    • (2001) Acta Crystallogr. , vol.D57 , pp. 957-967
    • Wojtczak, A.1    Neumann, P.2    Cody, V.3
  • 16
    • 0031297816 scopus 로고    scopus 로고
    • Crystal structure of rat transthyretin at 2.5 Å resolution: First report on a unique tetrameric structure
    • Wojtczak, A. (1997) Crystal structure of rat transthyretin at 2.5 Å resolution: First report on a unique tetrameric structure. Acta Biochim. Polon. 44, 505-518.
    • (1997) Acta Biochim. Polon. , vol.44 , pp. 505-518
    • Wojtczak, A.1
  • 17
    • 0034903745 scopus 로고    scopus 로고
    • Structure of rat transthyretin (rTTR) complex with thyroxine at 2.5 Å resolution: First non-biased insight into thyroxine binding reveals different hormone orientation in two binding sites
    • Wojtczak, A., Cody, V., Luft, J. & Pangborn, W. (2001) Structure of rat transthyretin (rTTR) complex with thyroxine at 2.5 Å resolution: First non-biased insight into thyroxine binding reveals different hormone orientation in two binding sites. Acta Crystalogr. D57, 1061-1070.
    • (2001) Acta Crystalogr. , vol.D57 , pp. 1061-1070
    • Wojtczak, A.1    Cody, V.2    Luft, J.3    Pangborn, W.4
  • 18
    • 0016428708 scopus 로고
    • Negative cooperativity in the binding of thyroxine to human serum transthyretin
    • Ferguson, R.N., Edeldoch, H., Saroff, H.A. & Robbins, J. (1975) Negative cooperativity in the binding of thyroxine to human serum transthyretin. Biochemistry 14, 282-289.
    • (1975) Biochemistry , vol.14 , pp. 282-289
    • Ferguson, R.N.1    Edeldoch, H.2    Saroff, H.A.3    Robbins, J.4
  • 19
    • 0017682858 scopus 로고
    • Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence
    • Cheng, S., Pages, R.A., Saroff, H.A., Edelhoch, H. & Robbins, J. (1977) Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence. Biochemistry 16, 3707-3713.
    • (1977) Biochemistry , vol.16 , pp. 3707-3713
    • Cheng, S.1    Pages, R.A.2    Saroff, H.A.3    Edelhoch, H.4    Robbins, J.5
  • 21
    • 0026573629 scopus 로고
    • Fluorescence study of the thyroxine-dependent conformational changes in human serum transthyretin
    • González, G. & Tapia, G. (1992) Fluorescence study of the thyroxine-dependent conformational changes in human serum transthyretin. FEBS Lett. 297, 253-256.
    • (1992) FEBS Lett. , vol.297 , pp. 253-256
    • González, G.1    Tapia, G.2
  • 22
    • 0024574326 scopus 로고
    • Fluorescent derivative of cysteine-10 reveals thyroxine-dependent conformational modifications in human serum prealbumin
    • González, G. (1989) Fluorescent derivative of cysteine-10 reveals thyroxine-dependent conformational modifications in human serum prealbumin. Arch. Biochem. Biophys. 271, 200-205.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 200-205
    • González, G.1
  • 25
    • 0033823859 scopus 로고    scopus 로고
    • Structure of human transthyretin complexed with bromophenols: A new mode of binding
    • Gosh, M., Meerts, I.A., Cook, A., Bergman, A., Brouwer, A. & Johnson, L.N. (2000) Structure of human transthyretin complexed with bromophenols: A new mode of binding. Acta Crystallogr. D56, 1085-1092.
    • (2000) Acta Crystallogr. , vol.D56 , pp. 1085-1092
    • Gosh, M.1    Meerts, I.A.2    Cook, A.3    Bergman, A.4    Brouwer, A.5    Johnson, L.N.6
  • 26
    • 4243470236 scopus 로고    scopus 로고
    • Novel binding mode of tetraiodothyroacetic acid in transthyretin
    • Submitted
    • Wojtczak, A., Neumann, P., Muziol, T. & Cody, V. (2001) Novel binding mode of tetraiodothyroacetic acid in transthyretin. Acta Crystallogr. D. Submitted.
    • (2001) Acta Crystallogr. D.
    • Wojtczak, A.1    Neumann, P.2    Muziol, T.3    Cody, V.4
  • 27
    • 0018217549 scopus 로고
    • Thyroxine-induced conformational changes in pre-albumin
    • Irace, G. & Edelhoch, H. (1978) Thyroxine-induced conformational changes in pre-albumin. Biochemistry 17, 5729-5733.
    • (1978) Biochemistry , vol.17 , pp. 5729-5733
    • Irace, G.1    Edelhoch, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.