Helix-helix packing in a membrane-like environment

Journal of Molecular Biology

Volumn 272, Issue 4, 1997, Pages 633-641

  Mingarro, Ismael ^a   Elofsson, Arne ^a   Von Heijne, Gunnar ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Glycophorin A; Helix packing; Membrane protein

Indexed keywords

DODECYL SULFATE SODIUM; GLYCOPHORIN A; MEMBRANE PROTEIN; MUTANT PROTEIN; TETRAMER;

AMINO ACID SEQUENCE; ARTICLE; DIMERIZATION; GENE INSERTION; MICELLE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE;

EID: 0031551579     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1276     Document Type: Article

References (19)

1. Abagyan, R. A., Totrov, M. M. & Kuznetsov, D. N. (1994). ICM: a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comput. Chem. 15, 488-506.
2. Adams, P. D., Arkin, I. T., Engelman, D. M. & Brünger, A. T. (1995). Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Struct. Biol. 2, 154-162.
3. Adams, P., Engelman, D. & Brünger, A. (1996). Improved prediction for the structure of a dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins: Struct. Funct. Genet. 26, 257-261.
4. Arkin, I. T., Rothman, M., Ludlam, C. F. C., Aimoto, S., Engelman, D. M., Rothschild, K. J. & Smith, S. O. (1995). Structural model of the phospholamban ion-channel complex in phospholipid membranes. J. Mol. Biol. 248, 824-834.
5. Connolly, M. J. (1983). Analytical molecular surface calculation. J. Appl. Crystallog. 16, 548-558.
6. Geisselsoder, J., Witney, F. & Yuckenberg, P. (1987). Efficient site-directed in vitro mutagenesis. BioTechniques, 5, 786-791.
7. Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl Crystallog. 24, 946-950.
8. Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA, 82, 488-492.
9. Langosch, D., Brosig, B., Kolmar, H. & Fritz, H. J. (1996). Dimerization of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263, 525-530.
10. Lemmon, M. A. & Engelman, D. M. (1994). Specificity and promiscuity in membrane helix interactions. Quart. Rev. Biophys. 27, 157-218.
11. Lemmon, M., Flanagan, J., Hunt, J., Adair, B., Bormann, B.-J., Dempsey, C. & Engelman, D. (1992a). Glycophorin A dimerization is driven by specific interactions between transmembrane α-helices. J. Biol. Chem. 267, 7683-7689.
12. Lemmon, M. A., Flanagan, J. M., Treutlein, H. R., Zhang, J. & Engelman, D. M. (1992b). Sequence specificity in the dimerization of transmembrane α-helices. Biochemistry, 31, 12719-12725.
13. Lemmon, M. A., Treutlein, H. R., Adams, P. D., Brünger, A. T. & Engelman, D. M. (1994). A dimerization motif for transmembrane α-helices. Nature Struct. Biol. 1, 157-163.
14. Li, S.-C. & Deber, C. M. (1994). A measure of helical propensity for amino acids in membrane environments. Nature Struct. Biol. 1, 368-373.
15. MacKenzie, K. R., Prestegard, J. H. & Engelman, D. M. (1997). A transmembrane helix dimer: structure and implications. Science, 276, 131-133.
16. Mingarro, I., Whitley, P., Lemmon, M. A. & von Heijne, G. (1996). Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: a rapid way to map helix-helix interactions in integral membrane proteins. Protein Sci. 5, 1339-1341.
17. Sharp, L. L., Zhou, J. & Blair, D. F. (1995a). Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis. Proc. Natl Acad. Sci. USA, 92, 7946-7950.
18. Sharp, L. L., Zhou, J. & Blair, D. F. (1995b). Tryptophan-scanning mutagenesis of MotB, an integral membrane protein essential for flagellar rotation in Escherichia coli. Biochemistry, 34, 9166-9171.
19. Treutlein, H. R., Lemmon, M. A., Engelman, D. M. & Brünger, A. T. (1992). The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices. Biochemistry, 31, 12726-12732.