메뉴 건너뛰기




Volumn 11, Issue 2, 2001, Pages 82-88

Coiled coils: A highly versatile protein folding motif

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; OLIGOMER; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 0035252931     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(00)01898-5     Document Type: Review
Times cited : (898)

References (64)
  • 1
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: A program for predicting two- and three-stranded coiled coils
    • (1997) Protein Sci. , vol.6 , pp. 1179-1189
    • Wolf, E.1
  • 3
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • (1998) Science , vol.282 , pp. 1462-1467
    • Harbury, P.B.1
  • 6
    • 0032055747 scopus 로고    scopus 로고
    • A distinct 14 residue site triggers coiled-coil formation in cortexillin I
    • (1998) Embo J. , vol.17 , pp. 1883-1891
    • Steinmetz, M.O.1
  • 7
    • 0030987241 scopus 로고    scopus 로고
    • Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. Implications for motor activity
    • (1997) J. Biol. Chem. , vol.272 , pp. 8946-8956
    • Tripet, B.1
  • 10
    • 0034697357 scopus 로고    scopus 로고
    • A distinct seven-residue trigger sequence is indispensable for proper coiled-coil formation of the human macrophage scavenger receptor oligomerization domain
    • (2000) J. Biol. Chem. , vol.275 , pp. 11672-11677
    • Frank, S.1
  • 11
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • (2000) Structure , vol.8 , pp. 223-230
    • Burkhard, P.1
  • 12
    • 0028959280 scopus 로고
    • Protein destabilization by electrostatic repulsions in the two-stranded alpha-helical coiled-coil/leucine zipper
    • (1995) Protein Sci. , vol.4 , pp. 237-250
    • Kohn, W.D.1
  • 13
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1
  • 15
    • 0034602397 scopus 로고    scopus 로고
    • Attractive interhelical electrostatic interactions in the PAR leucine zipper subfamily (VBP/TEF, HLF, and DBP) preclude heterodimerization with other B-ZIP subfamilies
    • (2000) J. Biol. Chem. , vol.275 , pp. 34826-34832
    • Moll, J.R.1
  • 16
    • 0032546758 scopus 로고    scopus 로고
    • Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids
    • (1998) J. Mol. Biol. , vol.279 , pp. 959-972
    • Krylov, D.1
  • 17
    • 0031764838 scopus 로고    scopus 로고
    • Surface salt bridges stabilize the GCN4 leucine zipper
    • (1998) Protein Sci. , vol.7 , pp. 2431-2437
    • Spek, E.J.1
  • 18
    • 0030700592 scopus 로고    scopus 로고
    • The conformation of the alpha-helical coiled coil domain of macrophage scavenger receptor is pH dependent
    • (1997) Biochemistry , vol.36 , pp. 15140-15146
    • Suzuki, K.1
  • 19
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1
  • 20
    • 0030996370 scopus 로고    scopus 로고
    • Design of a leucine zipper coiled coil stabilized 1.4 kcal mol-1 by phosphorylation of a serine in the e position
    • (1997) Protein Sci. , vol.6 , pp. 1273-1283
    • Szilak, L.1
  • 21
    • 0033615971 scopus 로고    scopus 로고
    • A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly
    • (1999) J. Cell Biol. , vol.147 , pp. 1039-1048
    • Liang, W.1
  • 22
    • 0033543220 scopus 로고    scopus 로고
    • 2+-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site
    • (1999) Biochemistry , vol.38 , pp. 10543-10551
    • Farah, C.S.1    Reinach, F.C.2
  • 23
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 154-162
    • Adams, P.D.1
  • 25
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly
    • (2000) J. Mol. Biol. , vol.298 , pp. 817-832
    • Herrmann, H.1
  • 26
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • (1999) J. Mol. Biol. , vol.286 , pp. 1403-1420
    • Herrmann, H.1
  • 27
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in alpha-helical coiled coils: Stutters and stammers
    • (1996) Proteins , vol.26 , pp. 134-145
    • Brown, J.H.1
  • 28
    • 0033793829 scopus 로고    scopus 로고
    • Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3539-3558
    • Wu, K.C.1
  • 29
    • 0028948876 scopus 로고
    • Tetrabrachion: A filamentous archaebacterial surface protein assembly of unusual structure and extreme stability
    • (1995) J. Mol. Biol. , vol.245 , pp. 385-401
    • Peters, J.1
  • 30
    • 0029942482 scopus 로고    scopus 로고
    • Hyperthermostable surface layer protein tetrabrachion from the archaebacterium Staphylothermus marinus: Evidence for the presence of a right-handed coiled coil derived from the primary structure
    • (1996) J. Mol. Biol. , vol.257 , pp. 1031-1041
    • Peters, J.1
  • 31
    • 0030156252 scopus 로고    scopus 로고
    • A hyperthermostable protease of the subtilisin family bound to the surface layer of the archaeon Staphylothermus marinus
    • (1996) Curr. Biol. , vol.6 , pp. 739-749
    • Mayr, J.1
  • 35
    • 0030872273 scopus 로고    scopus 로고
    • Two-state thermal unfolding of a long dimeric coiled-coil: The Acanthamoeba myosin II rod
    • (1997) Biochemistry , vol.36 , pp. 7876-7883
    • Zolkiewski, M.1
  • 37
    • 0031471243 scopus 로고    scopus 로고
    • The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    • (1997) Cell , vol.91 , pp. 985-994
    • Kozielski, F.1
  • 38
    • 0032559824 scopus 로고    scopus 로고
    • Role of the kinesin neck region in processive microtubule-based motility
    • (1998) J. Cell Biol. , vol.140 , pp. 1407-1416
    • Romberg, L.1
  • 39
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1
  • 40
    • 0032513004 scopus 로고    scopus 로고
    • Structural characterization of a dynein motor domain
    • (1998) J. Mol. Biol. , vol.276 , pp. 927-937
    • Samso, M.1
  • 42
    • 0030592549 scopus 로고    scopus 로고
    • Fifty ways to love your lever: Myosin motors
    • (1996) Cell , vol.87 , pp. 151-157
    • Block, S.M.1
  • 44
    • 0029068861 scopus 로고
    • Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella
    • (1995) J. Mol. Biol. , vol.250 , pp. 52-63
    • Burgess, S.A.1
  • 45
    • 0028172110 scopus 로고
    • The histidine interruption of an alpha-helical coiled coil allosterically mediates a pH-dependent ligand dissociation from macrophage scavenger receptors
    • (1994) J. Biol. Chem. , vol.269 , pp. 25598-25604
    • Doi, T.1
  • 46
    • 0033044710 scopus 로고    scopus 로고
    • Role of the buried glutamate in the alpha-helical coiled coil domain of the macrophage scavenger receptor
    • (1999) Biochemistry , vol.38 , pp. 1751-1756
    • Suzuki, K.1
  • 47
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1
  • 50
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1
  • 51
    • 0033749565 scopus 로고    scopus 로고
    • Testing the 3Q:1R 'Rule': Mutational analysis of the ionic 'Zero' layer in the yeast exocytic SNARE complex reveals no requirement for arginine
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3849-3858
    • Katz, L.1    Brennwald, P.2
  • 52
    • 0034669052 scopus 로고    scopus 로고
    • Exocytosis requires asymmetry in the central layer of the SNARE complex
    • (2000) Embo J. , vol.19 , pp. 6000-6010
    • Ossig, R.1
  • 53
    • 0033784541 scopus 로고    scopus 로고
    • Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 894-902
    • Munson, M.1
  • 55
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1
  • 56
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1
  • 57
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • (1993) J. Mol. Biol. , vol.233 , pp. 139-154
    • Konig, P.1    Richmond, T.J.2
  • 58
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1
  • 60
    • 0031883280 scopus 로고    scopus 로고
    • A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of c-fos
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 967-977
    • Ahn, S.1
  • 61
    • 0032493843 scopus 로고    scopus 로고
    • Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper
    • (1998) J. Mol. Biol. , vol.281 , pp. 165-181
    • Lavigne, P.1
  • 62
    • 0029563395 scopus 로고
    • Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerization
    • (1995) J. Mol. Biol. , vol.254 , pp. 505-520
    • Lavigne, P.1
  • 63
    • 0034682781 scopus 로고    scopus 로고
    • Modulation of the oligomerization state of the bovine F1-ATPase inhibitor protein, IF1, by pH
    • (2000) J. Biol. Chem. , vol.275 , pp. 25460-25464
    • Cabezon, E.1
  • 64
    • 85081160079 scopus 로고    scopus 로고
    • Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments
    • in press
    • J. Mol. Biol.
    • Strelkov, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.