메뉴 건너뛰기




Volumn 331, Issue 1, 2003, Pages 255-262

Sequence context strongly modulates association of polar residues in transmembrane helices

Author keywords

Helix helix interactions; M13 major coat protein; Polar residues in membranes; TOXCAT assay; Transmembrane helix

Indexed keywords

ASPARAGINE; ASPARTIC ACID; COAT PROTEIN; GLUTAMIC ACID; GLUTAMINE;

EID: 0038499536     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00714-9     Document Type: Article
Times cited : (72)

References (31)
  • 1
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J.L., Engelman D.M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry. 29:1990;4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 2
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma C., Gratkowski H., Lear J.D., DeGrado W.F. Asparagine-mediated self-association of a model transmembrane helix. Nature Struct. Biol. 7:2000;161-166.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 3
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H., Lear J.D., DeGrado W.F. Polar side chains drive the association of model transmembrane peptides. Proc. Natl Acad. Sci. USA. 98:2001;880-885.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 6
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson J.P., Weinger J.S., Engelman D.M. Motifs of serine and threonine can drive association of transmembrane helices. J. Mol. Biol. 316:2002;799-805.
    • (2002) J. Mol. Biol. , vol.316 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 7
    • 0034952420 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds in the CFTR membrane domain
    • Therien A.G., Grant F.E., Deber C.M. Interhelical hydrogen bonds in the CFTR membrane domain. Nature Struct. Biol. 8:2001;597-601.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 597-601
    • Therien, A.G.1    Grant, F.E.2    Deber, C.M.3
  • 8
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • Bargmann C.I., Hung M.C., Weinberg R.A. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell. 45:1986;649-657.
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 9
    • 0037133518 scopus 로고    scopus 로고
    • Polar residues in membrane domains of proteins: Molecular basis for helix-helix association in a mutant CFTR transmembrane segment
    • Partridge A.W., Melnyk R.A., Deber C.M. Polar residues in membrane domains of proteins: molecular basis for helix-helix association in a mutant CFTR transmembrane segment. Biochemistry. 41:2002;3647-3653.
    • (2002) Biochemistry , vol.41 , pp. 3647-3653
    • Partridge, A.W.1    Melnyk, R.A.2    Deber, C.M.3
  • 10
    • 0026511905 scopus 로고
    • A subdomain in the transmembrane domain is necessary for p185neu*activation
    • Cao H., Bangalore L., Bormann B.J., Stern D.F. A subdomain in the transmembrane domain is necessary for p185neu* activation. EMBO J. 11:1992;923-932.
    • (1992) EMBO J. , vol.11 , pp. 923-932
    • Cao, H.1    Bangalore, L.2    Bormann, B.J.3    Stern, D.F.4
  • 11
    • 0029881315 scopus 로고    scopus 로고
    • Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor
    • Smith S.O., Smith C.S., Bormann B.J. Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor. Nature Struct. Biol. 3:1996;252-258.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 252-258
    • Smith, S.O.1    Smith, C.S.2    Bormann, B.J.3
  • 12
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • Mendrola J.M., Berger M.B., King M.C., Lemmon M.A. The single transmembrane domains of ErbB receptors self-associate in cell membranes. J. Biol. Chem. 277:2002;4704-4712.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 13
    • 0030969251 scopus 로고    scopus 로고
    • Transmembrane domain sequence requirements for activation of the p185c-neu receptor tyrosine kinase
    • Chen L.I., Webster M.K., Meyer A.N., Donoghue D.J. Transmembrane domain sequence requirements for activation of the p185c-neu receptor tyrosine kinase. J. Cell. Biol. 137:1997;619-631.
    • (1997) J. Cell. Biol. , vol.137 , pp. 619-631
    • Chen, L.I.1    Webster, M.K.2    Meyer, A.N.3    Donoghue, D.J.4
  • 14
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes A., Gerstein M., Engelman D.M. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J. Mol. Biol. 296:2000;921-936.
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 18
    • 0025817412 scopus 로고
    • IgM antigen receptor complex contains phosphoprotein products of B29 and mb-1 genes
    • Campbell K.S., Hager E.J., Friedrich R.J., Cambier J.C. IgM antigen receptor complex contains phosphoprotein products of B29 and mb-1 genes. Proc. Natl Acad. Sci. USA. 88:1991;3982-3986.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3982-3986
    • Campbell, K.S.1    Hager, E.J.2    Friedrich, R.J.3    Cambier, J.C.4
  • 21
    • 0027143565 scopus 로고
    • Val→Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein
    • Deber C.M., Khan A.R., Li Z., Joensson C., Glibowicka M., Wang J. Val→Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Natl Acad. Sci. USA. 90:1993;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
  • 22
    • 0036298185 scopus 로고    scopus 로고
    • Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophage
    • Melnyk R.A., Partridge A.W., Deber C.M. Transmembrane domain mediated self-assembly of major coat protein subunits from Ff bacteriophage. J. Mol. Biol. 315:2002;63-72.
    • (2002) J. Mol. Biol. , vol.315 , pp. 63-72
    • Melnyk, R.A.1    Partridge, A.W.2    Deber, C.M.3
  • 23
    • 0032577317 scopus 로고    scopus 로고
    • The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane
    • Haigh N.G., Webster R.E. The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane. J. Mol. Biol. 279:1998;19-29.
    • (1998) J. Mol. Biol. , vol.279 , pp. 19-29
    • Haigh, N.G.1    Webster, R.E.2
  • 24
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ W.P., Engelman D.M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl Acad. Sci. USA. 96:1999;863-868.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 25
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:1992;487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 27
    • 33845551411 scopus 로고
    • Geometry of the imino-carbonyl (NH-O=C) hydrogen bond. 1. Lone-pair directionality
    • Taylor R., Kennard O., Versichel W. Geometry of the imino-carbonyl (NH-O=C) hydrogen bond. 1. Lone-pair directionality. J. Am. Chem. Soc. 105:1983;5761-5766.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5761-5766
    • Taylor, R.1    Kennard, O.2    Versichel, W.3
  • 28
    • 84977288315 scopus 로고
    • Geometry of the NH-OC hydrogen bond. 3. Hydrogen bond distances and angles
    • Taylor R., Kennard O., Versichel W. Geometry of the NH-OC hydrogen bond. 3. Hydrogen bond distances and angles. Acta Crystallog. sect. B. 40:1984;280-288.
    • (1984) Acta Crystallog. sect. B , vol.40 , pp. 280-288
    • Taylor, R.1    Kennard, O.2    Versichel, W.3
  • 29
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T-cell receptor-CD3 complex
    • Call M.E., Pyrdol J., Wiedmann M., Wucherpfennig K.W. The organizing principle in the formation of the T-cell receptor-CD3 complex. Cell. 111:2002;967-979.
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 30
    • 0029060799 scopus 로고
    • Artificial transmembrane segments. Requirements for stop transfer and polypeptide orientation
    • Chen H., Kendall D.A. Artificial transmembrane segments. Requirements for stop transfer and polypeptide orientation. J. Biol. Chem. 270:1995;14115-14122.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14115-14122
    • Chen, H.1    Kendall, D.A.2
  • 31
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucl. Acids Res. 27:1999;49-54.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.