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Volumn 20, Issue 3, 2012, Pages 397-405

Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; APC6 PROTEIN; CHAPERONE; CYTOSOL RECEPTOR; INVASION PLASMID GENE C PROTEIN; LIGAND; MAMA PROTEIN; PEROXIN 5 PROTEIN; PROTOZOAL PROTEIN; PTS1 PROTEIN; PTS2 PROTEIN; UNCLASSIFIED DRUG;

EID: 84857933257     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.01.006     Document Type: Review
Times cited : (263)

References (34)
  • 1
    • 42449161827 scopus 로고    scopus 로고
    • The interface of protein-protein complexes: Analysis of contacts and prediction of interactions
    • DOI 10.1007/s00018-007-7451-x
    • Bahadur, R.P., and Zacharias, M. (2008). The interface of protein-protein complexes: analysis of contacts and prediction of interactions. Cell. Mol. Life Sci. 65, 1059-1072. (Pubitemid 351563896)
    • (2008) Cellular and Molecular Life Sciences , vol.65 , Issue.7-8 , pp. 1059-1072
    • Bahadur, R.P.1    Zacharias, M.2
  • 2
    • 34848823742 scopus 로고    scopus 로고
    • Mitochondrial protein-import machinery: correlating structure with function
    • DOI 10.1016/j.tcb.2007.07.010, PII S0962892407001699
    • Baker, M.J., Frazier, A.E., Gulbis, J.M., and Ryan, M.T. (2007). Mitochondrial protein-import machinery: correlating structure with function. Trends Cell Biol. 17, 456-464. (Pubitemid 47499044)
    • (2007) Trends in Cell Biology , vol.17 , Issue.9 , pp. 456-464
    • Baker, M.J.1    Frazier, A.E.2    Gulbis, J.M.3    Ryan, M.T.4
  • 3
    • 33747856166 scopus 로고    scopus 로고
    • The MPI Bioinformatics Toolkit for protein sequence analysis
    • Biegert, A., Mayer, C., Remmert, M., Söding, J., and Lupas, A.N. (2006). The MPI Bioinformatics Toolkit for protein sequence analysis. Nucleic Acids Res. 34 (Web Server issue), W335-W339.
    • (2006) Nucleic Acids Res , vol.34 , Issue.WEB SERVER ISSUE
    • Biegert, A.1    Mayer, C.2    Remmert, M.3    Söding, J.4    Lupas, A.N.5
  • 4
    • 80054856259 scopus 로고    scopus 로고
    • DARPins and other repeat protein scaffolds: Advances in engineering and applications
    • Boersma, Y.L., and Plückthun, A. (2011). DARPins and other repeat protein scaffolds: advances in engineering and applications. Curr. Opin.Biotechnol. 22, 849-857.
    • (2011) Curr. Opin.Biotechnol. , vol.22 , pp. 849-857
    • Boersma, Y.L.1    Plückthun, A.2
  • 5
    • 33845300838 scopus 로고    scopus 로고
    • Peroxisome targeting signal 1: Is it really a simple tripeptide?
    • DOI 10.1016/j.bbamcr.2006.08.022, PII S016748890600228X, Peroxisomes: Morphology, Function, Biogenesis and Disorders
    • Brocard, C., and Hartig, A. (2006). Peroxisome targeting signal 1: is it really a simple tripeptide? Biochim. Biophys. Acta 1763, 1565-1573. (Pubitemid 44880463)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.12 , pp. 1565-1573
    • Brocard, C.1    Hartig, A.2
  • 6
    • 42449136263 scopus 로고    scopus 로고
    • Designed TPR modules as novel anticancer agents
    • Cortajarena, A.L., Yi, F., and Regan, L. (2008). Designed TPR modules as novel anticancer agents. ACS Chem. Biol. 3, 161-166.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 161-166
    • Cortajarena, A.L.1    Yi, F.2    Regan, L.3
  • 7
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • DOI 10.1016/j.tibs.2003.10.007
    • D'Andrea, L.D., and Regan, L. (2003). TPR proteins: the versatile helix. Trends Biochem. Sci. 28, 655-662. (Pubitemid 37500900)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.12 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 8
    • 33645093201 scopus 로고    scopus 로고
    • Tetratricopeptide repeats in the type III secretion chaperone, LcrH: Their role in substrate binding and secretion
    • Edqvist, P.J., Bröms, J.E., Betts, H.J., Forsberg, A., Pallen, M.J., and Francis, M.S. (2006). Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion. Mol. Microbiol. 59, 31-44.
    • (2006) Mol. Microbiol. , vol.59 , pp. 31-44
    • Edqvist, P.J.1    Bröms, J.E.2    Betts, H.J.3    Forsberg, A.4    Pallen, M.J.5    Francis, M.S.6
  • 10
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: The proteomics server for in-depth protein knowledge and analysis
    • DOI 10.1093/nar/gkg563
    • Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R.D., and Bairoch, A. (2003). ExPASy: The proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31, 3784-3788. (Pubitemid 37442246)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5    Bairoch, A.6
  • 12
    • 0342576245 scopus 로고    scopus 로고
    • A proposed model for the PEX5-peroxisomal targeting signal-1 recognition complex
    • DOI 10.1002/(SICI)1097-0134(20000215)38:3<241::AID-PROT1>3.0.CO;2-1
    • Gatto, G.J., Jr., Geisbrecht, B.V., Gould, S.J., and Berg, J.M. (2000). A proposed model for the PEX5-peroxisomal targeting signal-1 recognition complex. Proteins 38, 241-246. (Pubitemid 30084334)
    • (2000) Proteins: Structure, Function and Genetics , vol.38 , Issue.3 , pp. 241-246
    • Gatto Jr., G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 13
  • 14
    • 34447540060 scopus 로고    scopus 로고
    • Crystal structure of YrrB: A TPR protein with an unusual peptide-binding site
    • DOI 10.1016/j.bbrc.2007.06.129, PII S0006291X07013848
    • Han, D., Oh, J., Kim, K., Lim, H., and Kim, Y. (2007). Crystal structure of YrrB: a TPR protein with an unusual peptide-binding site. Biochem. Biophys. Res. Commun. 360, 784-790. (Pubitemid 47082437)
    • (2007) Biochemical and Biophysical Research Communications , vol.360 , Issue.4 , pp. 784-790
    • Han, D.1    Oh, J.2    Kim, K.3    Lim, H.4    Kim, Y.5
  • 15
    • 63449132045 scopus 로고    scopus 로고
    • Redesign of a protein-peptide interaction: Characterization and applications
    • Jackrel, M.E., Valverde, R., and Regan, L. (2009). Redesign of a protein-peptide interaction: characterization and applications. Protein Science 18, 762-774.
    • (2009) Protein Science , vol.18 , pp. 762-774
    • Jackrel, M.E.1    Valverde, R.2    Regan, L.3
  • 16
    • 70350465130 scopus 로고    scopus 로고
    • Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins
    • Javadi, Y., and Main, E.R.G. (2009). Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins. Proc. Natl. Acad. Sci. USA 106, 17383-17388.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17383-17388
    • Javadi, Y.1    Main, E.R.G.2
  • 17
    • 34250796909 scopus 로고    scopus 로고
    • Structure and stability of designed TPR protein superhelices: Unusual crystal packing and implications for natural TPR proteins
    • DOI 10.1107/S0907444907024353, PII S0907444907024353
    • Kajander, T., Cortajarena, A.L., Mochrie, S., and Regan, L. (2007). Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins. Acta Crystallogr. D Biol. Crystallogr. 63, 800-811. (Pubitemid 46975670)
    • (2007) Acta Crystallographica Section D: Biological Crystallography , vol.63 , Issue.7 , pp. 800-811
    • Kajander, T.1    Cortajarena, A.L.2    Mochrie, S.3    Regan, L.4
  • 18
    • 30544453079 scopus 로고    scopus 로고
    • Crystal structure of PilF: Functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
    • DOI 10.1016/j.bbrc.2005.12.108, PII S0006291X05028524
    • Kim, K., Oh, J., Han, D., Kim, E.E., Lee, B., and Kim, Y. (2006). Crystal structure of PilF: functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa. Biochem. Biophys. Res. Commun. 340, 1028-1038. (Pubitemid 43083382)
    • (2006) Biochemical and Biophysical Research Communications , vol.340 , Issue.4 , pp. 1028-1038
    • Kim, K.1    Oh, J.2    Han, D.3    Kim, E.E.4    Lee, B.5    Kim, Y.6
  • 19
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • Letunic, I., Doerks, T., and Bork, P. (2011). SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40 (Database issue), D302-D305.
    • (2011) Nucleic Acids Res. , vol.40 , Issue.DATABASE ISSUE
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 20
    • 75849126506 scopus 로고    scopus 로고
    • The structural basis of peptide-protein binding strategies
    • London, N., Movshovitz-Attias, D., and Schueler-Furman, O. (2010). The structural basis of peptide-protein binding strategies. Structure 18, 188-199.
    • (2010) Structure , vol.18 , pp. 188-199
    • London, N.1    Movshovitz-Attias, D.2    Schueler-Furman, O.3
  • 21
    • 67649861394 scopus 로고    scopus 로고
    • IpaB-IpgC interaction defines binding motif for type III secretion translocator
    • Lunelli, M., Lokareddy, R.K., Zychlinsky, A., and Kolbe, M. (2009). IpaB-IpgC interaction defines binding motif for type III secretion translocator. Proc. Natl. Acad. Sci. USA 106, 9661-9666.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinsky, A.3    Kolbe, M.4
  • 22
    • 67649556148 scopus 로고    scopus 로고
    • Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria
    • Mirus, O., Bionda, T., von Haeseler, A., and Schleiff, E. (2009). Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria. J. Mol. Model. 15, 971-982.
    • (2009) J. Mol. Model. , vol.15 , pp. 971-982
    • Mirus, O.1    Bionda, T.2    Von Haeseler, A.3    Schleiff, E.4
  • 24
    • 77953573815 scopus 로고    scopus 로고
    • Sub-angstrom modeling of complexes between flexible peptides and globular proteins
    • Raveh, B., London, N., and Schueler-Furman, O. (2010). Sub-angstrom modeling of complexes between flexible peptides and globular proteins. Proteins 78, 2029-2040.
    • (2010) Proteins , vol.78 , pp. 2029-2040
    • Raveh, B.1    London, N.2    Schueler-Furman, O.3
  • 25
    • 79955716232 scopus 로고    scopus 로고
    • Rosetta FlexPepDock ab-initio: Simultaneous folding, docking and refinement of peptides onto their receptors
    • Raveh, B., London, N., Zimmerman, L., and Schueler-Furman, O. (2011). Rosetta FlexPepDock ab-initio: simultaneous folding, docking and refinement of peptides onto their receptors. PLoS ONE 6, e18934.
    • (2011) PLoS ONE , vol.6
    • Raveh, B.1    London, N.2    Zimmerman, L.3    Schueler-Furman, O.4
  • 26
    • 48449100534 scopus 로고    scopus 로고
    • Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5
    • Sampathkumar, P., Roach, C., Michels, P.A., and Hol, W.G. (2008). Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5. J. Mol. Biol. 381, 867-880.
    • (2008) J. Mol. Biol. , vol.381 , pp. 867-880
    • Sampathkumar, P.1    Roach, C.2    Michels, P.A.3    Hol, W.G.4
  • 27
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • DOI 10.1016/S0092-8674(00)80830-2
    • Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F.U., and Moarefi, I. (2000). Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210. (Pubitemid 32004747)
    • (2000) Cell , vol.101 , Issue.2 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl F.Ulrich7    Moarefi, I.8
  • 29
    • 70350457561 scopus 로고    scopus 로고
    • Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host
    • Tiwari, D., Singh, R.K., Goswami, K., Verma, S.K., Prakash, B., and Nandicoori, V.K. (2009). Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host. J. Biol. Chem. 284, 27467-27479.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27467-27479
    • Tiwari, D.1    Singh, R.K.2    Goswami, K.3    Verma, S.K.4    Prakash, B.5    Nandicoori, V.K.6
  • 30
    • 69949190148 scopus 로고    scopus 로고
    • Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure
    • Wang, J., Dye, B.T., Rajashankar, K.R., Kurinov, I., and Schulman, B.A. (2009). Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure. Nat. Struct. Mol. Biol. 16, 987-989.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 987-989
    • Wang, J.1    Dye, B.T.2    Rajashankar, K.R.3    Kurinov, I.4    Schulman, B.A.5
  • 31
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • DOI 10.1016/j.tibs.2003.08.009, PII S0968000403002184
    • Young, J.C., Barral, J.M., and Ulrich Hartl, F. (2003). More than folding: localized functions of cytosolic chaperones. Trends Biochem. Sci. 28, 541-547. (Pubitemid 38366280)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.10 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Hartl, F.U.3
  • 34
    • 78149281017 scopus 로고    scopus 로고
    • The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27
    • Zhang, Z., Kulkarni, K., Hanrahan, S.J., Thompson, A.J., and Barford, D. (2010). The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27. EMBO J. 29, 3733-3744.
    • (2010) EMBO J. , vol.29 , pp. 3733-3744
    • Zhang, Z.1    Kulkarni, K.2    Hanrahan, S.J.3    Thompson, A.J.4    Barford, D.5


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