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Volumn 16, Issue 11, 2007, Pages 2552-2559

A high-resolution solution structure of a trypanosomatid FYVE domain

Author keywords

FYVE; Membrane trafficking; NMR structure; Residual dipolar couplings

Indexed keywords

FYVE DOMAIN CONTAINING PROTEIN; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 35648948473     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073009807     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartels, C., Xia, T.H., Billeter, M., Guntert, P., and Wuthrich, K. 1995. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J. Biomol. NMR 6: 1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Guntert, P.4    Wuthrich, K.5
  • 4
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai, M.L., Huang, Y., Sakaguchi, K., Clore, G.M., Gronenborn, A.M., and Craigie, R. 1998. An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11: 97-102.
    • (1998) J. Biomol. NMR , vol.11 , pp. 97-102
    • Cai, M.L.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 6
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free R, and complete crossvalidation for dipolar coupling refinement of NMR structures
    • Clore, G.M. and Garrett, D.S. 1999. R-factor, free R, and complete crossvalidation for dipolar coupling refinement of NMR structures. J. Am. Chem. Soc. 121: 9008-9012.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 7
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 8
    • 0345700741 scopus 로고    scopus 로고
    • Computer modeling of the membrane interaction of FYVE domains
    • Diraviyam, K., Stahelin, R.V., Cho, W., and Murray, D. 2003. Computer modeling of the membrane interaction of FYVE domains. J. Mol. Biol. 328: 721-736.
    • (2003) J. Mol. Biol , vol.328 , pp. 721-736
    • Diraviyam, K.1    Stahelin, R.V.2    Cho, W.3    Murray, D.4
  • 12
    • 0034637460 scopus 로고    scopus 로고
    • Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes - Role of conserved residues
    • Gaullier, J.M., Ronning, E., Gillooly, D.J., and Stenmark, H. 2000. Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes - Role of conserved residues. J. Biol. Chem. 275: 24595-24600.
    • (2000) J. Biol. Chem , vol.275 , pp. 24595-24600
    • Gaullier, J.M.1    Ronning, E.2    Gillooly, D.J.3    Stenmark, H.4
  • 14
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C., and Wuthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283-298.
    • (1997) J. Mol. Biol , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 15
    • 33748751597 scopus 로고    scopus 로고
    • TbVps34, the trypanosome orthologue of Vps34, is required for Golgi complex segregation
    • Hall, B.S., Gabernet-Castello, C., Voak, A., Goulding, D., Natesan, S.K., and Field, M.C. 2006. TbVps34, the trypanosome orthologue of Vps34, is required for Golgi complex segregation. J. Biol. Chem. 281: 27600-27612.
    • (2006) J. Biol. Chem , vol.281 , pp. 27600-27612
    • Hall, B.S.1    Gabernet-Castello, C.2    Voak, A.3    Goulding, D.4    Natesan, S.K.5    Field, M.C.6
  • 16
    • 0034130999 scopus 로고    scopus 로고
    • Filamentous bacteriophage for aligning RNA, DNA, and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions
    • Hansen, M.R., Hanson, P., and Pardi, A. 2000. Filamentous bacteriophage for aligning RNA, DNA, and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions. Methods Enzymol. 317: 220-240.
    • (2000) Methods Enzymol , vol.317 , pp. 220-240
    • Hansen, M.R.1    Hanson, P.2    Pardi, A.3
  • 18
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Guntert, P., and Wuthrich, K. 2002. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319: 209-227.
    • (2002) J. Mol. Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 19
    • 29144477132 scopus 로고    scopus 로고
    • A FYVE-containing unusual cyclic nucleotide phosphodiesterase from Trypanosoma cruzi
    • Kunz, S., Oberholzer, M., and Seebeck, T. 2005. A FYVE-containing unusual cyclic nucleotide phosphodiesterase from Trypanosoma cruzi. FEBS J. 272: 6412-6422.
    • (2005) FEBS J , vol.272 , pp. 6412-6422
    • Kunz, S.1    Oberholzer, M.2    Seebeck, T.3
  • 20
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
    • Kuszewski, J., Gronenborn, A.M., and Clore, G.M. 1996. Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Sci. 5: 1067-1080.
    • (1996) Protein Sci , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 21
    • 33748329427 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain
    • Kutateladze, T.G. 2006. Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain. Biochim. Biophys. Acta 1761: 868-877.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 868-877
    • Kutateladze, T.G.1
  • 22
    • 0035793903 scopus 로고    scopus 로고
    • Structural mechanism of endosome docking by the FYVE domain
    • Kutateladze, T. and Overduin, M. 2001. Structural mechanism of endosome docking by the FYVE domain. Science 291: 1793-1796.
    • (2001) Science , vol.291 , pp. 1793-1796
    • Kutateladze, T.1    Overduin, M.2
  • 26
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • Mao, Y.X., Nickitenko, A., Duan, X.Q., Lloyd, T.E., Wu, M.N., Bellen, H., and Quiocho, F.A. 2000. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 100: 447-456.
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.X.1    Nickitenko, A.2    Duan, X.Q.3    Lloyd, T.E.4    Wu, M.N.5    Bellen, H.6    Quiocho, F.A.7
  • 28
    • 26844441149 scopus 로고    scopus 로고
    • Validating the use of database potentials in protein structure determination by NMR
    • Mertens, H.D.T. and Gooley, P.R. 2005. Validating the use of database potentials in protein structure determination by NMR. FEBS Lett. 579: 5542-5548.
    • (2005) FEBS Lett , vol.579 , pp. 5542-5548
    • Mertens, H.D.T.1    Gooley, P.R.2
  • 29
    • 0033612372 scopus 로고    scopus 로고
    • Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
    • Misra, S. and Hurley, J.H. 1999. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell 97: 657-666.
    • (1999) Cell , vol.97 , pp. 657-666
    • Misra, S.1    Hurley, J.H.2
  • 32
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • Stahelin, R.V., Long, F., Diraviyam, K., Bruzik, K.S., Murray, D., and Cho, W. 2002. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277: 26379-26388.
    • (2002) J. Biol. Chem , vol.277 , pp. 26379-26388
    • Stahelin, R.V.1    Long, F.2    Diraviyam, K.3    Bruzik, K.S.4    Murray, D.5    Cho, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.