메뉴 건너뛰기




Volumn 383, Issue 3, 2008, Pages 455-464

Crystal-Structure and Biochemical Characterization of Recombinant Human Calcyphosine Delineates a Novel EF-Hand-Containing Protein Family

Author keywords

calcium signaling; calcium binding protein; calcyphosine; crystal structure; EF hand

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM BINDING PROTEIN; CALCIUM ION; CALMODULIN; CYCLIC AMP; PHOSPHATIDYLINOSITOL; PROTEIN CALCYPHOSINE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 52949149317     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.048     Document Type: Article
Times cited : (17)

References (33)
  • 1
    • 0026661582 scopus 로고
    • Physiological and pathological regulation of thyroid cell proliferation and differentiation by thyrotropin and other factors
    • Dumont J.E., Lamy F., Roger P., and Maenhaut C. Physiological and pathological regulation of thyroid cell proliferation and differentiation by thyrotropin and other factors. Physiol. Rev. 72 (1992) 667-697
    • (1992) Physiol. Rev. , vol.72 , pp. 667-697
    • Dumont, J.E.1    Lamy, F.2    Roger, P.3    Maenhaut, C.4
  • 2
    • 0024446194 scopus 로고
    • Cloning and sequencing of a calcium-binding protein regulated by cyclic AMP in the thyroid
    • Lefort A., Lecocq R., Libert F., Lamy F., Swillens S., Vassart G., and Dumont J.E. Cloning and sequencing of a calcium-binding protein regulated by cyclic AMP in the thyroid. EMBO J. 8 (1989) 111-116
    • (1989) EMBO J. , vol.8 , pp. 111-116
    • Lefort, A.1    Lecocq, R.2    Libert, F.3    Lamy, F.4    Swillens, S.5    Vassart, G.6    Dumont, J.E.7
  • 3
    • 0018598139 scopus 로고
    • Pattern of protein phosphorylation in intact stimulated cells: thyrotropin and dog thyroid
    • Lecocq R., Lamy F., and Dumont J.E. Pattern of protein phosphorylation in intact stimulated cells: thyrotropin and dog thyroid. Eur. J. Biochem. 102 (1979) 147-152
    • (1979) Eur. J. Biochem. , vol.102 , pp. 147-152
    • Lecocq, R.1    Lamy, F.2    Dumont, J.E.3
  • 4
    • 0025289728 scopus 로고
    • Use of two-dimensional gel electrophoresis and autoradiography as a tool in cell biology: the example of the thyroid and the liver
    • Lecocq R., Lamy F., and Dumont J.E. Use of two-dimensional gel electrophoresis and autoradiography as a tool in cell biology: the example of the thyroid and the liver. Electrophoresis 11 (1990) 200-212
    • (1990) Electrophoresis , vol.11 , pp. 200-212
    • Lecocq, R.1    Lamy, F.2    Dumont, J.E.3
  • 5
    • 0027483732 scopus 로고
    • R2D5 antigen: a calcium-binding phosphoprotein predominantly expressed in olfactory receptor neurons
    • Nemoto Y., Ikeda J., Katoh K., Koshimoto H., Yoshihara Y., and Mori K. R2D5 antigen: a calcium-binding phosphoprotein predominantly expressed in olfactory receptor neurons. J. Cell Biol. 123 (1993) 963-976
    • (1993) J. Cell Biol. , vol.123 , pp. 963-976
    • Nemoto, Y.1    Ikeda, J.2    Katoh, K.3    Koshimoto, H.4    Yoshihara, Y.5    Mori, K.6
  • 6
    • 34249888765 scopus 로고    scopus 로고
    • Identification of novel biomarkers in pediatric primitive neuroectodermal tumors and ependymomas by proteome-wide analysis
    • de Bont J.M., den Boer M.L., Kros J.M., Passier M.M., Reddingius R.E., Smitt P.A., et al. Identification of novel biomarkers in pediatric primitive neuroectodermal tumors and ependymomas by proteome-wide analysis. J. Neuropathol. Exp. Neurol. 66 (2007) 505-516
    • (2007) J. Neuropathol. Exp. Neurol. , vol.66 , pp. 505-516
    • de Bont, J.M.1    den Boer, M.L.2    Kros, J.M.3    Passier, M.M.4    Reddingius, R.E.5    Smitt, P.A.6
  • 7
    • 0037130942 scopus 로고    scopus 로고
    • Genomic structure of the sponge, Halichondria okadai calcyphosine gene
    • Yuasa H.J., Nakatomi A., Suzuki T., and Yazawa M. Genomic structure of the sponge, Halichondria okadai calcyphosine gene. Gene 298 (2002) 21-27
    • (2002) Gene , vol.298 , pp. 21-27
    • Yuasa, H.J.1    Nakatomi, A.2    Suzuki, T.3    Yazawa, M.4
  • 9
    • 0028876764 scopus 로고
    • Rapid purification and identification of calcyphosine, a Ca(2 +)-binding protein phosphorylated by protein kinase A
    • Lecocq R., Lamy F., Erneux C., and Dumont J.E. Rapid purification and identification of calcyphosine, a Ca(2 +)-binding protein phosphorylated by protein kinase A. Biochem. J. 306 Pt 1 (1995) 147-151
    • (1995) Biochem. J. , vol.306 , Issue.PART 1 , pp. 147-151
    • Lecocq, R.1    Lamy, F.2    Erneux, C.3    Dumont, J.E.4
  • 10
  • 12
    • 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
  • 14
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. Sect. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 16
    • 0032923758 scopus 로고    scopus 로고
    • Crystal structure of recombinant bovine neurocalcin
    • Vijay-Kumar S., and Kumar V.D. Crystal structure of recombinant bovine neurocalcin. Nat. Struct. Biol. 6 (1999) 80-88
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 80-88
    • Vijay-Kumar, S.1    Kumar, V.D.2
  • 17
    • 0030998285 scopus 로고    scopus 로고
    • Structure of a calpain Ca(2 +)-binding domain reveals a novel EF-hand and Ca(2 +)-induced conformational changes
    • Blanchard H., Grochulski P., Li Y., Arthur J.S., Davies P.L., Elce J.S., and Cygler M. Structure of a calpain Ca(2 +)-binding domain reveals a novel EF-hand and Ca(2 +)-induced conformational changes. Nat. Struct. Biol. 4 (1997) 532-538
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 532-538
    • Blanchard, H.1    Grochulski, P.2    Li, Y.3    Arthur, J.S.4    Davies, P.L.5    Elce, J.S.6    Cygler, M.7
  • 18
    • 0035798666 scopus 로고    scopus 로고
    • Calcium-regulated DNA binding and oligomerization of the neuronal calcium-sensing protein, calsenilin/DREAM/KChIP3
    • Osawa M., Tong K.I., Lilliehook C., Wasco W., Buxbaum J.D., Cheng H.Y., et al. Calcium-regulated DNA binding and oligomerization of the neuronal calcium-sensing protein, calsenilin/DREAM/KChIP3. J. Biol. Chem. 276 (2001) 41005-41013
    • (2001) J. Biol. Chem. , vol.276 , pp. 41005-41013
    • Osawa, M.1    Tong, K.I.2    Lilliehook, C.3    Wasco, W.4    Buxbaum, J.D.5    Cheng, H.Y.6
  • 19
    • 0033520296 scopus 로고    scopus 로고
    • Dimerization of guanylyl cyclase-activating protein and a mechanism of photoreceptor guanylyl cyclase activation
    • Olshevskaya E.V., Ermilov A.N., and Dizhoor A.M. Dimerization of guanylyl cyclase-activating protein and a mechanism of photoreceptor guanylyl cyclase activation. J. Biol. Chem. 274 (1999) 25583-25587
    • (1999) J. Biol. Chem. , vol.274 , pp. 25583-25587
    • Olshevskaya, E.V.1    Ermilov, A.N.2    Dizhoor, A.M.3
  • 20
    • 0036468522 scopus 로고    scopus 로고
    • The functions of Ca(2 +) in bacteria: a role for EF-hand proteins?
    • Michiels J., Xi C., Verhaert J., and Vanderleyden J. The functions of Ca(2 +) in bacteria: a role for EF-hand proteins?. Trends Microbiol. 10 (2002) 87-93
    • (2002) Trends Microbiol. , vol.10 , pp. 87-93
    • Michiels, J.1    Xi, C.2    Verhaert, J.3    Vanderleyden, J.4
  • 21
    • 14844282775 scopus 로고    scopus 로고
    • Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins
    • Gentry H.R., Singer A.U., Betts L., Yang C., Ferrara J.D., Sondek J., and Parise L.V. Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins. J. Biol. Chem. 280 (2005) 8407-8415
    • (2005) J. Biol. Chem. , vol.280 , pp. 8407-8415
    • Gentry, H.R.1    Singer, A.U.2    Betts, L.3    Yang, C.4    Ferrara, J.D.5    Sondek, J.6    Parise, L.V.7
  • 23
    • 0142242192 scopus 로고    scopus 로고
    • The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana
    • Nagae M., Nozawa A., Koizumi N., Sano H., Hashimoto H., Sato M., and Shimizu T. The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana. J. Biol. Chem. 278 (2003) 42240-42246
    • (2003) J. Biol. Chem. , vol.278 , pp. 42240-42246
    • Nagae, M.1    Nozawa, A.2    Koizumi, N.3    Sano, H.4    Hashimoto, H.5    Sato, M.6    Shimizu, T.7
  • 24
    • 0036359353 scopus 로고    scopus 로고
    • Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins
    • Yap K.L., Ames J.B., Swindells M.B., and Ikura M. Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins. Methods Mol. Biol. 173 (2002) 317-324
    • (2002) Methods Mol. Biol. , vol.173 , pp. 317-324
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 25
    • 0141594755 scopus 로고    scopus 로고
    • A closed compact structure of native Ca(2 +)-calmodulin
    • Fallon J.L., and Quiocho F.A. A closed compact structure of native Ca(2 +)-calmodulin. Structure 11 (2003) 1303-1307
    • (2003) Structure , vol.11 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 26
    • 0027429963 scopus 로고
    • Three-dimensional structure of recoverin, a calcium sensor in vision
    • Flaherty K.M., Zozulya S., Stryer L., and McKay D.B. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75 (1993) 709-716
    • (1993) Cell , vol.75 , pp. 709-716
    • Flaherty, K.M.1    Zozulya, S.2    Stryer, L.3    McKay, D.B.4
  • 27
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum C.L., Yan S.Z., Bard J., Shen Y.Q., Lu D., Soelaiman S., et al. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415 (2002) 396-402
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1    Yan, S.Z.2    Bard, J.3    Shen, Y.Q.4    Lu, D.5    Soelaiman, S.6
  • 28
    • 0035823139 scopus 로고    scopus 로고
    • Target-induced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca(2 +)/calmodulin-dependent kinase kinase peptide
    • Kurokawa H., Osawa M., Kurihara H., Katayama N., Tokumitsu H., Swindells M.B., et al. Target-induced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca(2 +)/calmodulin-dependent kinase kinase peptide. J. Mol. Biol. 312 (2001) 59-68
    • (2001) J. Mol. Biol. , vol.312 , pp. 59-68
    • Kurokawa, H.1    Osawa, M.2    Kurihara, H.3    Katayama, N.4    Tokumitsu, H.5    Swindells, M.B.6
  • 29
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
    • Meador W.E., Means A.R., and Quiocho F.A. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257 (1992) 1251-1255
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 32
    • 33749246223 scopus 로고    scopus 로고
    • Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode
    • Maximciuc A.A., Putkey J.A., Shamoo Y., and Mackenzie K.R. Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode. Structure 14 (2006) 1547-1556
    • (2006) Structure , vol.14 , pp. 1547-1556
    • Maximciuc, A.A.1    Putkey, J.A.2    Shamoo, Y.3    Mackenzie, K.R.4
  • 33
    • 25144469471 scopus 로고    scopus 로고
    • Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin
    • Guo Q., Shen Y., Lee Y.S., Gibbs C.S., Mrksich M., and Tang W.J. Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin. EMBO J. 24 (2005) 3190-3201
    • (2005) EMBO J. , vol.24 , pp. 3190-3201
    • Guo, Q.1    Shen, Y.2    Lee, Y.S.3    Gibbs, C.S.4    Mrksich, M.5    Tang, W.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.