메뉴 건너뛰기




Volumn 5, Issue 11, 1997, Pages 1453-1464

A new triple-stranded α-helical bundle in solution: The assembling of the cytosolic tail of MHC-associated invariant chain

Author keywords

Invariant chain; NMR structure; Protein trafficking; Protein protein recognition; helical bundle

Indexed keywords


EID: 0030828144     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00295-5     Document Type: Article
Times cited : (16)

References (61)
  • 3
    • 0027177971 scopus 로고
    • Metal iondependent modulation of a designed protein
    • Handel, T.M., Williams, S.A. & DeGrado, W.F. (1993). Metal iondependent modulation of a designed protein. Science 241, 879-885.
    • (1993) Science , vol.241 , pp. 879-885
    • Handel, T.M.1    Williams, S.A.2    DeGrado, W.F.3
  • 6
    • 0028309466 scopus 로고
    • Engineering of betabellin 14D: Disulfide-induced folding of a •-sheet protein
    • Yan, Y. & Erickson, B.W. (1994). Engineering of betabellin 14D: disulfide-induced folding of a •-sheet protein. Protein Sci. 3, 1069-1073.
    • (1994) Protein Sci. , vol.3 , pp. 1069-1073
    • Yan, Y.1    Erickson, B.W.2
  • 8
    • 0025990386 scopus 로고
    • Spectroscopic investigation of structure in octarellin (a de novo protein designed to adopt the •/•-barrel packing)
    • Beauregard, M., et al., & Martial, J.A. (1991). Spectroscopic investigation of structure in octarellin (a de novo protein designed to adopt the •/•-barrel packing). Protein Eng. 4, 745-749.
    • (1991) Protein Eng. , vol.4 , pp. 745-749
    • Beauregard, M.1    Martial, J.A.2
  • 10
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from first principles
    • Regan, L. & DeGrado, W.F. (1988). Characterization of a helical protein designed from first principles. Science 241, 976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    DeGrado, W.F.2
  • 12
    • 0005906960 scopus 로고
    • Secondary structure of the designed peptide alpha-1 determined by nuclear magnetic resonance spectroscopy
    • Ciesla, D.J., Gilbert, D.E. & Feigon, J. (1991). Secondary structure of the designed peptide alpha-1 determined by nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 113, 3957-3961.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 3957-3961
    • Ciesla, D.J.1    Gilbert, D.E.2    Feigon, J.3
  • 13
    • 0027416662 scopus 로고
    • Crystal structure of a synthetic triple-stranded •-helical bundle
    • Lovejoy, B., et al., & Eisenberg, D. (1993). Crystal structure of a synthetic triple-stranded •-helical bundle. Science 259, 1288-1293.
    • (1993) Science , vol.259 , pp. 1288-1293
    • Lovejoy, B.1    Eisenberg, D.2
  • 14
    • 0028858475 scopus 로고
    • Structure-activity relationship of the leucine-based sorting motifs in the cytosolic tail of the MHC-associated invariant chain
    • Motta, A., Bremnes, B., Castiglione Morelli, M.A., Frank, R.W., Saviano, G. & Bakke, O. (1995). Structure-activity relationship of the leucine-based sorting motifs in the cytosolic tail of the MHC-associated invariant chain. J. Biol. Chem. 270, 27165-27171.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27165-27171
    • Motta, A.1    Bremnes, B.2    Castiglione Morelli, M.A.3    Frank, R.W.4    Saviano, G.5    Bakke, O.6
  • 15
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a strong signal for endosomal compartments
    • Bakke, O. & Dobberstein, B. (1990). MHC class II-associated invariant chain contains a strong signal for endosomal compartments. Cell 63, 707-716.
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 16
    • 0027498929 scopus 로고
    • Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments
    • Romagnoli, P., Layet, C., Yewdell, J., Bakke, O. & Germain, R.N. (1993). Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments. J. Exp. Med. 177, 583-596.
    • (1993) J. Exp. Med. , vol.177 , pp. 583-596
    • Romagnoli, P.1    Layet, C.2    Yewdell, J.3    Bakke, O.4    Germain, R.N.5
  • 17
    • 0027525192 scopus 로고
    • The role of the cytoplasmic tail of MHC class II associated invariant chain in targeting to and retention in endocytic compartments
    • Pieters, J., Bakke, O. & Dobberstein, B. (1993). The role of the cytoplasmic tail of MHC class II associated invariant chain in targeting to and retention in endocytic compartments. J. Cell Sci. 106, 831-846.
    • (1993) J. Cell Sci. , vol.106 , pp. 831-846
    • Pieters, J.1    Bakke, O.2    Dobberstein, B.3
  • 18
    • 0028229612 scopus 로고
    • A LI and a ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalisation
    • Bremnes, B., Madsen, T., Gedde-Dahl, M. & Bakke, O. (1994). A LI and a ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalisation. J. Cell Biol. 107, 2021-2032.
    • (1994) J. Cell Biol. , vol.107 , pp. 2021-2032
    • Bremnes, B.1    Madsen, T.2    Gedde-Dahl, M.3    Bakke, O.4
  • 19
    • 0029148781 scopus 로고
    • A role for acidic residues in di-leucine motif-based targeting to endocytic pathway
    • Pond, L., et al., & Peterson, P.A. (1995). A role for acidic residues in di-leucine motif-based targeting to endocytic pathway. J. Biol. Chem. 270, 19989-19997.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19989-19997
    • Pond, L.1    Peterson, P.A.2
  • 20
    • 0028861481 scopus 로고
    • Invariant chain induces a delayed transport from early to late endosomes
    • Gorvel, J.-P., Escola, J.-M., Stang, E. & Bakke, O. (1995). Invariant chain induces a delayed transport from early to late endosomes. J. Biol. Chem. 270, 2741-2746.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2741-2746
    • Gorvel, J.-P.1    Escola, J.-M.2    Stang, E.3    Bakke, O.4
  • 23
    • 33748233229 scopus 로고    scopus 로고
    • Electrospray mass spectrometry of biomacromolecular complexes with noncovalent interactions - New analytical perspectives for supramolecular chemistry and molecular recognition processes
    • Przybylski, M. & Glocker, M.O. (1996). Electrospray mass spectrometry of biomacromolecular complexes with noncovalent interactions - new analytical perspectives for supramolecular chemistry and molecular recognition processes. Angew. Chem. Int. Ed. Engl. 35, 806-826.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 806-826
    • Przybylski, M.1    Glocker, M.O.2
  • 24
  • 25
    • 0028174033 scopus 로고
    • Fingerprinting G-protein-coupled receptors
    • Attwood, T.K. & Findlay, J.B.C. (1994). Fingerprinting G-protein-coupled receptors. Protein Eng. 7, 195-203.
    • (1994) Protein Eng. , vol.7 , pp. 195-203
    • Attwood, T.K.1    Findlay, J.B.C.2
  • 26
    • 0030926720 scopus 로고    scopus 로고
    • The three dimensional structure of aquaporin-1
    • Walz, T., et al., & Engel, A. (1997). The three dimensional structure of aquaporin-1. Nature 387, 624-627.
    • (1997) Nature , vol.387 , pp. 624-627
    • Walz, T.1    Engel, A.2
  • 27
    • 0031011374 scopus 로고    scopus 로고
    • Three-dimensional organization of a human water channel
    • Cheng, A., van Hoek, A.N., Yeager, M., Verkman, A.S. & Mitra, A.K. (1997). Three-dimensional organization of a human water channel. Nature 387, 627-630.
    • (1997) Nature , vol.387 , pp. 627-630
    • Cheng, A.1    Van Hoek, A.N.2    Yeager, M.3    Verkman, A.S.4    Mitra, A.K.5
  • 28
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D. & Stewart, M. (1975). Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98, 293-299.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-299
    • McLachlan, A.D.1    Stewart, M.2
  • 29
    • 0000920828 scopus 로고
    • The packing of •-helices: Simple coiled-coils
    • Crick, F.H.C. (1953). The packing of •-helices: simple coiled-coils. Acta Cryst. 6, 689-697.
    • (1953) Acta Cryst. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 30
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S. & Alber, T. (1993). A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 31
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim, W.A. & Sauer, R.T. (1991). The role of internal packing interactions in determining the structure and stability of a protein. J. Mol. Biol. 219, 359-365.
    • (1991) J. Mol. Biol. , vol.219 , pp. 359-365
    • Lim, W.A.1    Sauer, R.T.2
  • 32
    • 0026532266 scopus 로고
    • Design and structural analysis of alternative hydrophobic core packing arrangement in bacteriophage T4 lysozyme
    • Hurley, J.H., Baase, W.A. & Matthews, B.W. (1992). Design and structural analysis of alternative hydrophobic core packing arrangement in bacteriophage T4 lysozyme. J. Mol. Biol. 224, 1143-1159.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1143-1159
    • Hurley, J.H.1    Baase, W.A.2    Matthews, B.W.3
  • 33
    • 0025879501 scopus 로고
    • In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core
    • Stites, W.E., Gittis, A.G., Lattman, E.E. & Shortle, D. (1991). In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core. J. Mol. Biol. 221, 7-14.
    • (1991) J. Mol. Biol. , vol.221 , pp. 7-14
    • Stites, W.E.1    Gittis, A.G.2    Lattman, E.E.3    Shortle, D.4
  • 34
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J.U., Luthy, R. & Eisenberg, D. (1991). A method to identify protein sequences that fold into a known three-dimensional structure. Science 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 35
    • 0025083334 scopus 로고
    • Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigen
    • Marks, M.S., Blum, J.S. & Cresswell, P. (1990). Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigen. J. Cell. Biol. 111, 839-855.
    • (1990) J. Cell. Biol. , vol.111 , pp. 839-855
    • Marks, M.S.1    Blum, J.S.2    Cresswell, P.3
  • 36
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • Pfeffer, S.R. & Rothman, J.E. (1987). Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 56, 892-905.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 892-905
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 37
    • 0027248612 scopus 로고
    • Oligomerization of a membrane protein correlates with its retention in the Golgi complex
    • Weisz, O.A., Swift, A.M. & Mackhamer, C.E. (1993). Oligomerization of a membrane protein correlates with its retention in the Golgi complex. J. Cell Biol. 122, 1185-1196.
    • (1993) J. Cell Biol. , vol.122 , pp. 1185-1196
    • Weisz, O.A.1    Swift, A.M.2    Mackhamer, C.E.3
  • 38
    • 0028047115 scopus 로고
    • Kin recognition between medial Golgi enzymes in HeLa cells
    • Nilsson, T., et al., & Warren, G. (1994). Kin recognition between medial Golgi enzymes in HeLa cells. EMBO J. 13, 562-574.
    • (1994) EMBO J. , vol.13 , pp. 562-574
    • Nilsson, T.1    Warren, G.2
  • 39
    • 0029890064 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells
    • Nilsson, T., Rabouille, C., Hui, N.,Watson, R. & Warren, G. (1996). The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells. J.Cell Sci. 109, 1975-1989.
    • (1996) J.Cell Sci. , vol.109 , pp. 1975-1989
    • Nilsson, T.1    Rabouille, C.2    Hui, N.3    Watson, R.4    Warren, G.5
  • 40
    • 0028233882 scopus 로고
    • Mapping the functional regions in the lumenal domain of the class II-associated invariant chain
    • Bijlmakers, M.E., Benaroch, P. & Ploegh, H.L. (1994). Mapping the functional regions in the lumenal domain of the class II-associated invariant chain. J. Exp. Med. 180, 623-629.
    • (1994) J. Exp. Med. , vol.180 , pp. 623-629
    • Bijlmakers, M.E.1    Benaroch, P.2    Ploegh, H.L.3
  • 41
    • 0030887458 scopus 로고    scopus 로고
    • Exon 6 is essential for invariant chain trimerization and induction of large endosomal structures
    • Gedde-Dahl, M., Freisewinkel, I., Staschewski, M., Schenck, K., Koch, N. & Bakke, O. (1997). Exon 6 is essential for invariant chain trimerization and induction of large endosomal structures. J Biol. Chem. 272, 8281-8287.
    • (1997) J Biol. Chem. , vol.272 , pp. 8281-8287
    • Gedde-Dahl, M.1    Freisewinkel, I.2    Staschewski, M.3    Schenck, K.4    Koch, N.5    Bakke, O.6
  • 42
    • 0031586326 scopus 로고    scopus 로고
    • MHC class II associated invariant chain induced enlarged endosomal structures. A morphological study
    • Stang, E. & Bakke, O. (1997). MHC class II associated invariant chain induced enlarged endosomal structures. A morphological study. Exptl. Cell Res. 235, 79-92.
    • (1997) Exptl. Cell Res. , vol.235 , pp. 79-92
    • Stang, E.1    Bakke, O.2
  • 43
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. (1979). Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 44
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application of proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R.R. (1983). Coherence transfer by isotropic mixing: application of proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 47
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D.G. (1985). MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-366.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-366
    • Bax, A.1    Davis, D.G.2
  • 48
    • 0000883197 scopus 로고
    • Nonselective three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment
    • Vuister, G.W., Boelens, R. & Kaptein, R. (1988). Nonselective three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment. J. Magn. Reson. 80, 176-183.
    • (1988) J. Magn. Reson. , vol.80 , pp. 176-183
    • Vuister, G.W.1    Boelens, R.2    Kaptein, R.3
  • 49
    • 0023882968 scopus 로고
    • Three-dimensional NMR spectroscopy of a protein in solution
    • Oschkinat, H., et al., & Clore, G.M. (1988). Three-dimensional NMR spectroscopy of a protein in solution. Nature 332, 374-376.
    • (1988) Nature , vol.332 , pp. 374-376
    • Oschkinat, H.1    Clore, G.M.2
  • 50
    • 0001766053 scopus 로고
    • Observation of spin diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy
    • Boelens, R., Vuister, G.W., Koning, T.M.G. & Kaptein, R. (1989). Observation of spin diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy. J. Am. Chem. Soc. 111, 8525-8526.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8525-8526
    • Boelens, R.1    Vuister, G.W.2    Koning, T.M.G.3    Kaptein, R.4
  • 51
    • 0000758233 scopus 로고
    • 3D NOE-NOE spectroscopy of proteins. Observation of sequential 3D NOE cross peaks in arc repressor
    • Breg, J., Boelens, R., Vuister, G.W. & Kaptein, R. (1990). 3D NOE-NOE spectroscopy of proteins. Observation of sequential 3D NOE cross peaks in arc repressor. J. Magn. Reson. 87, 646-651.
    • (1990) J. Magn. Reson. , vol.87 , pp. 646-651
    • Breg, J.1    Boelens, R.2    Vuister, G.W.3    Kaptein, R.4
  • 52
    • 44949290542 scopus 로고
    • Calculation of the nuclear Overhauser effect and the determination of proton-proton distances in the presence of internal motions
    • Koning, T.M.G., Boelens, R. & Kaptein, R. (1990). Calculation of the nuclear Overhauser effect and the determination of proton-proton distances in the presence of internal motions. J. Magn. Reson. 90, 111-123.
    • (1990) J. Magn. Reson. , vol.90 , pp. 111-123
    • Koning, T.M.G.1    Boelens, R.2    Kaptein, R.3
  • 53
    • 0021757436 scopus 로고
    • A new force field for molecular mechanical simulation of nucleic acids and proteins
    • Weiner, S.J., et al., & Weiner P.K. (1984). A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106, 765-784.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 765-784
    • Weiner, S.J.1    Weiner, P.K.2
  • 54
    • 0000291225 scopus 로고
    • Optimized intermolecular potential functions for liquid alcohols
    • Jorgensen, W.L. (1986). Optimized intermolecular potential functions for liquid alcohols. J. Phys. Chem. 90, 1276-1284.
    • (1986) J. Phys. Chem. , vol.90 , pp. 1276-1284
    • Jorgensen, W.L.1
  • 55
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W.L & Tirado-Rives, J. (1988). The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110, 1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 56
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motions of a system with constraints: Molecular dynamics of n-alcanes
    • Ryckaert, J.P., Ciccotti, G. & Berendsen, H.J.C. (1977). Numerical integration of the Cartesian equations of motions of a system with constraints: molecular dynamics of n-alcanes. J. Comp. Phys. 23, 327-341.
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 57
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • van Gunsteren, W.F. & Berendsen, H.J.C. (1977). Algorithms for macromolecular dynamics and constraint dynamics. Mol. Phys. 34, 1311-1327.
    • (1977) Mol. Phys. , vol.34 , pp. 1311-1327
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 58
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990). WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 60
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 61
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts, S.G., Goldberg, M.S., Havel, T.F. & Wagner, G. (1992). The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci. 1, 736-751.
    • (1992) Protein Sci. , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.