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Volumn 77, Issue 3, 1999, Pages 1609-1618

Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; GLYCINE; MEMBRANE PROTEIN;

EID: 0032817780     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77009-8     Document Type: Article
Times cited : (240)

References (38)
  • 1
    • 0026785292 scopus 로고
    • Functional consequences of alterations to Gly-310, Gly-770, and Gly-801 located in the transmembrane domain of the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Andersen, J. P., B. Vilsen, and D. H. MacLennan. 1992. Functional consequences of alterations to Gly-310, Gly-770, and Gly-801 located in the transmembrane domain of the Ca(2+)-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 267:2767-2774.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2767-2774
    • Andersen, J.P.1    Vilsen, B.2    MacLennan, D.H.3
  • 2
    • 0028173780 scopus 로고
    • Rules for α-helix termination by glycine
    • Aurora, R., R. Srinivasan, and G. D. Rose. 1994. Rules for α-helix termination by glycine. Science. 264:1126-1130.
    • (1994) Science. , vol.264 , pp. 1126-1130
    • Aurora, R.1    Srinivasan, R.2    Rose, G.D.3
  • 3
    • 0024557054 scopus 로고
    • Synthetic peptides mimic the assembly of transmembrane glycoproteins
    • Bormann, B. J., W. J. Knowles, and V. T. Marchesi. 1989. Synthetic peptides mimic the assembly of transmembrane glycoproteins. J. Biol. Chem. 264:4033-4037.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4033-4037
    • Bormann, B.J.1    Knowles, W.J.2    Marchesi, V.T.3
  • 4
    • 0031563818 scopus 로고    scopus 로고
    • Helix packing in membrane proteins
    • Bovvie, J. U. 1997a. Helix packing in membrane proteins. J. Mol. Biol. 272:780-789.
    • (1997) J. Mol. Biol. , vol.272 , pp. 780-789
    • Bovvie, J.U.1
  • 5
    • 0030683493 scopus 로고    scopus 로고
    • Helix packing angle preferences
    • Bowie, J. U. 1997b. Helix packing angle preferences. Nat. Struct. Biol. 4:915-917.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 915-917
    • Bowie, J.U.1
  • 6
    • 0030614530 scopus 로고    scopus 로고
    • Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
    • Burke, C. L., M. A. Lemmon, B. A. Coren, D. M. Engelman, and D. F. Stern. 1997. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene. 14:687-696.
    • (1997) Oncogene. , vol.14 , pp. 687-696
    • Burke, C.L.1    Lemmon, M.A.2    Coren, B.A.3    Engelman, D.M.4    Stern, D.F.5
  • 7
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia, C. 1975. Structural invariants in protein folding. Nature. 254: 304-308.
    • (1975) Nature. , vol.254 , pp. 304-308
    • Chothia, C.1
  • 8
    • 0343063933 scopus 로고
    • Structure of proteins: Packing of alpha-helices and pleated sheets
    • Chothia, C., M. Levitt, and D. Richardson. 1977. Structure of proteins: packing of alpha-helices and pleated sheets. Proc. Natl. Acad. Sci. USA. 74:4130-4134.
    • (1977) Proc. Natl. Acad. Sci. USA. , vol.74 , pp. 4130-4134
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 10
    • 0026485306 scopus 로고
    • Role of transmembrane domain interactions in the assembly of class II MHC molecules
    • Cosson, P., and J. S. Bonifacino. 1992. Role of transmembrane domain interactions in the assembly of class II MHC molecules. Science. 258: 659-662.
    • (1992) Science. , vol.258 , pp. 659-662
    • Cosson, P.1    Bonifacino, J.S.2
  • 11
    • 0022995724 scopus 로고
    • Amino acid composition of the membrane and aqueous domains of integral membrane proteins
    • Deber, C. M., C. J. Brandi, R. B. Deber, L. C. Hsu, and X. K. Young. 1986. Amino acid composition of the membrane and aqueous domains of integral membrane proteins. Arch. Biochem. Biophys. 251:68-76.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 68-76
    • Deber, C.M.1    Brandi, C.J.2    Deber, R.B.3    Hsu, L.C.4    Young, X.K.5
  • 12
    • 0027143565 scopus 로고
    • Val→ Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein
    • Deber, C. M., A. R. Khan, Z. Li, C. Joensson, M. Glibowicka, and J. Wang. 1993. Val→ Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Natl. Acad. Sci. USA. 90:11648-11652.
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 11648-11652
    • Deber, C.M.1    Khan, A.R.2    Li, Z.3    Joensson, C.4    Glibowicka, M.5    Wang, J.6
  • 14
    • 0028978764 scopus 로고
    • The occurrence of C-H⋯O hydrogen bonds in proteins
    • Derewenda, Z. S., L. Lee, and U. Derewenda. 1995. The occurrence of C-H⋯O hydrogen bonds in proteins. J. Mol. Biol. 252:248-262.
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, U.3
  • 16
  • 17
    • 0031471113 scopus 로고    scopus 로고
    • The C9 methyl group of retinal interacts with glycine-121 in rhodopsin
    • Han, M., M. Groesbeek, T. P. Sakmar, and S. O. Smith. 1997. The C9 methyl group of retinal interacts with glycine-121 in rhodopsin. Proc. Natl. Acad. Sci. USA. 94:13442-13447.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 13442-13447
    • Han, M.1    Groesbeek, M.2    Sakmar, T.P.3    Smith, S.O.4
  • 18
    • 0029753237 scopus 로고    scopus 로고
    • The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin
    • Han, M., S. W. Lin, S. O. Smith, and T. P. Sakmar. 1996. The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin. J. Biol. Client. 271:32330-32336.
    • (1996) J. Biol. Client. , vol.271 , pp. 32330-32336
    • Han, M.1    Lin, S.W.2    Smith, S.O.3    Sakmar, T.P.4
  • 20
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the trans-membrane segments of human type i single span membrane proteins
    • Landolt-Marticorena, C., K. A. Williams, C. M. Deber, and R. A. Reithmeier. 1993. Non-random distribution of amino acids in the trans-membrane segments of human type I single span membrane proteins. J. Mol. Biol. 229:602-608.
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.4
  • 21
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M. A., and D. M. Engelman. 1994. Specificity and promiscuity in membrane helix interactions. Quart. Rev. Biophys. 27:157-218.
    • (1994) Quart. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 23
  • 25
    • 0026760920 scopus 로고
    • Glycine and β-branched residues support and modulate peptide helicity in membrane environments
    • Li, S. C., and C. M. Deber. 1992. Glycine and β-branched residues support and modulate peptide helicity in membrane environments. FEBS Lett. 311:217-220.
    • (1992) FEBS Lett. , vol.311 , pp. 217-220
    • Li, S.C.1    Deber, C.M.2
  • 26
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., J. H. Prestegard, and D. M. Engelman. 1997. A transmembrane helix dimer: structure and implications. Science. 276: 131-133.
    • (1997) Science. , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 27
    • 0027293043 scopus 로고
    • The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain
    • Millar, D. G., and G. C. Shore. 1993. The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain. J. Biol. Chem. 268:18403-18406.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18403-18406
    • Millar, D.G.1    Shore, G.C.2
  • 28
    • 0022631926 scopus 로고
    • The folding type of a protein is relevant to the amino acid composition
    • Nakashima, H., K. Nishikawa, and T. Ooi. 1986. The folding type of a protein is relevant to the amino acid composition. J. Biochem. (Tokyo). 99:153-162.
    • (1986) J. Biochem. (Tokyo). , vol.99 , pp. 153-162
    • Nakashima, H.1    Nishikawa, K.2    Ooi, T.3
  • 29
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T., and W. F. DeGrado. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:646-651.
    • (1990) Science. , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 31
    • 0023927904 scopus 로고
    • Identification of structural motifs from protein coordinate data: Secondary structure and first-level supersecondary structure
    • Richards, F. M., and C. E. Kundrot. 1988. Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure. Proteins. 3:71-84.
    • (1988) Proteins. , vol.3 , pp. 71-84
    • Richards, F.M.1    Kundrot, C.E.2
  • 32
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson, J. S., and D. C. Richardson. 1988. Amino acid preferences for specific locations at the ends of alpha helices. Science. 240:1648-1652.
    • (1988) Science. , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 33
    • 0028814024 scopus 로고
    • Determination of helix-helix interactions in membranes by rotational resonance NMR
    • Smith, S. O., and B. J. Bormann. 1995. Determination of helix-helix interactions in membranes by rotational resonance NMR. Proc. Natl. Acad. Sci. USA. 92:488-491.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 488-491
    • Smith, S.O.1    Bormann, B.J.2
  • 34
    • 0024976405 scopus 로고
    • Neu receptor dimerization
    • Sternberg, M. J., and W. J. Gullick. 1989. Neu receptor dimerization. Nature. 339:587.
    • (1989) Nature. , vol.339 , pp. 587
    • Sternberg, M.J.1    Gullick, W.J.2
  • 35
    • 0025274249 scopus 로고
    • A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization
    • Sternberg, M. J., and W. J. Gullick. 1990. A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization. Protein Eng. 3:245-248.
    • (1990) Protein Eng. , vol.3 , pp. 245-248
    • Sternberg, M.J.1    Gullick, W.J.2
  • 37
    • 0030983047 scopus 로고    scopus 로고
    • Architecture of helix bundle membrane proteins: An analysis of cytochrome c oxidase from bovine mitochondria
    • Wallin, E., T. Tsukihara, S. Yoshikawa, G. Von Heijne, and A. Elofsson. 1997. Architecture of helix bundle membrane proteins: an analysis of cytochrome c oxidase from bovine mitochondria. Protein Sci. 6:808-815.
    • (1997) Protein Sci. , vol.6 , pp. 808-815
    • Wallin, E.1    Tsukihara, T.2    Yoshikawa, S.3    Von Heijne, G.4    Elofsson, A.5
  • 38
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: The helical lattice superposition model
    • Walther, D., F. Eisenhaber, and P. Argos. 1996. Principles of helix-helix packing in proteins: the helical lattice superposition model. J. Mol. Biol. 255:536-553.
    • (1996) J. Mol. Biol. , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.