메뉴 건너뛰기




Volumn 262, Issue 1, 1999, Pages 1-11

Motor proteins of the kinesin family. Structures, variations, and nucleotide binding sites

Author keywords

Kar3; Kinesin crystal structure; Kinesin dimer; Motor protein; Ncd dimer; Nucleotide dependent conformations; P loop

Indexed keywords

KINESIN;

EID: 0033563154     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00341.x     Document Type: Short Survey
Times cited : (86)

References (52)
  • 1
    • 0033563024 scopus 로고    scopus 로고
    • Motor and cargo interactions
    • 1. Sheetz, M.P. (1999) Motor and cargo interactions. Eur. J. Biochem. 262, 19-25.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 19-25
    • Sheetz, M.P.1
  • 2
    • 0033563155 scopus 로고    scopus 로고
    • Microtubule motors in spindle and chromosome motility
    • 2. Endow, S.A. (1999) Microtubule motors in spindle and chromosome motility. Eur. J. Biochem. 262, 12-18.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 12-18
    • Endow, S.A.1
  • 4
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • 4. Hirokawa, N. (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 5
    • 0032410805 scopus 로고    scopus 로고
    • The case for a common ancestor: Kinesin and myosin motor proteins and G proteins
    • 5. Kull, F.J., Vale, R.D. & Fletterick, R. (1998) The case for a common ancestor: kinesin and myosin motor proteins and G proteins. J. Muscle Res. Cell Motil. 19, 877-886.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 877-886
    • Kull, F.J.1    Vale, R.D.2    Fletterick, R.3
  • 6
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • 6. Kull, F.J., Sablin, E., Lau, P., Fletterick, R. & Vale, R. (1996) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380, 550-554.
    • (1996) Nature , vol.380 , pp. 550-554
    • Kull, F.J.1    Sablin, E.2    Lau, P.3    Fletterick, R.4    Vale, R.5
  • 9
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor Ncd
    • 9. Sablin, E.P., Kull, F.J., Cooke, R., Vale, R.D. & Fletterick, R.J. (1996) Crystal structure of the motor domain of the kinesin-related motor Ncd. Nature 380, 555-559.
    • (1996) Nature , vol.380 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 11
    • 0032539526 scopus 로고    scopus 로고
    • X-ray crystal structure of the yeast KAR3 motor domain complexed with MgADP to 2.3 Å resolution
    • 11. Gulick, A., Song, H., Endow, S. & Rayment, I. (1998) X-ray crystal structure of the yeast KAR3 motor domain complexed with MgADP to 2.3 Å resolution. Biochemistry 37, 1769-1776.
    • (1998) Biochemistry , vol.37 , pp. 1769-1776
    • Gulick, A.1    Song, H.2    Endow, S.3    Rayment, I.4
  • 12
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
    • 12. Yang, J., Laymon, R. & Goldstein, L. (1989) A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell 56, 879-889.
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.1    Laymon, R.2    Goldstein, L.3
  • 14
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
    • 14. Case, R.B., Pierce, D.W., Hom-Booher, N., Hart, C.L. & Vale, R.D. (1997) The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. Cell 90, 959-966.
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom-Booher, N.3    Hart, C.L.4    Vale, R.D.5
  • 15
    • 0030924142 scopus 로고    scopus 로고
    • Reversal of the direction of movement of a molecular motor
    • 15. Henningsen, U. & Schliwa, M. (1997) Reversal of the direction of movement of a molecular motor. Nature 389, 93-96.
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 16
    • 0032555532 scopus 로고    scopus 로고
    • Determinants of kinesin motor polarity
    • 16. Endow, S.A. & Waligora, K.W. (1998) Determinants of kinesin motor polarity. Science 281, 1200-1202.
    • (1998) Science , vol.281 , pp. 1200-1202
    • Endow, S.A.1    Waligora, K.W.2
  • 17
    • 0030987241 scopus 로고    scopus 로고
    • Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides - Implications for motor activity
    • 17. Tripet, B., Vale, R.D. & Hodges, R.S. (1997) Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides - implications for motor activity. J. Biol. Chem. 272, 8946-8956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8946-8956
    • Tripet, B.1    Vale, R.D.2    Hodges, R.S.3
  • 18
    • 0031016939 scopus 로고    scopus 로고
    • Identification of kinesin neck region as a stable alpha-helical coiled coil and its thermodynamic characterization
    • 18. Morii, H., Takenawa, T., Arisaka, F. & Shimizu, T. (1997) Identification of kinesin neck region as a stable alpha-helical coiled coil and its thermodynamic characterization. Biochemistry 36, 1933-1942.
    • (1997) Biochemistry , vol.36 , pp. 1933-1942
    • Morii, H.1    Takenawa, T.2    Arisaka, F.3    Shimizu, T.4
  • 20
    • 0345055326 scopus 로고    scopus 로고
    • Conformations of kinesin: solution vs. crystal structures and interactions with microtubules
    • 20. Marx, A., Thormählen, M., Müller, J., Sack, S., Mandelkow, E.-M. & Mandelkow, E. (1998) Conformations of kinesin: solution vs. crystal structures and interactions with microtubules. Eur. Biophys. J. 27, 455-465.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 455-465
    • Marx, A.1    Thormählen, M.2    Müller, J.3    Sack, S.4    Mandelkow, E.-M.5    Mandelkow, E.6
  • 22
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstruction of microtubules decorated with monomeric and dimeric kinesins: Comparison with X-ray structure and implications for motility
    • 22. Hoenger, A., Sack, S., Thormählen, M., Marx, A., Müller, J., Gross, H. & Mandelkow, E. (1998) Image reconstruction of microtubules decorated with monomeric and dimeric kinesins: comparison with X-ray structure and implications for motility. J. Cell Biol. 141, 419-430.
    • (1998) J. Cell Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormählen, M.3    Marx, A.4    Müller, J.5    Gross, H.6    Mandelkow, E.7
  • 23
    • 0032559824 scopus 로고    scopus 로고
    • Role of the kinesin neck region in processive microtubule-based motility
    • 23. Romberg, L., Pierce, D. & Vale, R. (1998) Role of the kinesin neck region in processive microtubule-based motility. J. Cell Biol. 140, 1407-1416.
    • (1998) J. Cell Biol. , vol.140 , pp. 1407-1416
    • Romberg, L.1    Pierce, D.2    Vale, R.3
  • 25
    • 0030584675 scopus 로고    scopus 로고
    • Deciphering the alphabet of G proteins: The structure of the αβγ-heterotrimer
    • 25. Wittinghofer, A. (1996) Deciphering the alphabet of G proteins: The structure of the αβγ-heterotrimer. Structure 4, 357-361.
    • (1996) Structure , vol.4 , pp. 357-361
    • Wittinghofer, A.1
  • 26
    • 0030835649 scopus 로고    scopus 로고
    • Structural aspects of heterotrimeric G-protein signaling
    • 26. Bohm, A., Gaudet, R. & Sigler, P.B. (1997) Structural aspects of heterotrimeric G-protein signaling. Curr. Opin. Biotech. 8, 480-487.
    • (1997) Curr. Opin. Biotech. , vol.8 , pp. 480-487
    • Bohm, A.1    Gaudet, R.2    Sigler, P.B.3
  • 27
    • 0030920782 scopus 로고    scopus 로고
    • G-protein mechanisms: Insights from structural analysis
    • 27. Sprang, S.R. (1997) G-protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639-678,.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 28
    • 0031193924 scopus 로고    scopus 로고
    • Structural studies on myosin-II: Communication between distant protein domains
    • 28. Gulick, A.M. & Rayment, I. (1997) Structural studies on myosin-II: communication between distant protein domains. Bioessays 19, 561-569.
    • (1997) Bioessays , vol.19 , pp. 561-569
    • Gulick, A.M.1    Rayment, I.2
  • 29
    • 0030267349 scopus 로고    scopus 로고
    • Switches, latches, and amplifiers: Common themes of G proteins and molecular motors
    • 29. Vale, R.D. (1996) Switches, latches, and amplifiers: common themes of G proteins and molecular motors. J. Cell Biol. 135, 291-302.
    • (1996) J. Cell Biol. , vol.135 , pp. 291-302
    • Vale, R.D.1
  • 31
    • 0030036699 scopus 로고    scopus 로고
    • Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins
    • 31. Mittal, R., Ahmadian, M.R., Goody, R.S. & Wittinghofer, A. (1996) Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins. Science 273, 115-117.
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, R.S.3    Wittinghofer, A.4
  • 32
  • 33
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • 33. Holmes, K.C. (1997) The swinging lever-arm hypothesis of muscle contraction. Current Biol. 7, R112-R118.
    • (1997) Current Biol. , vol.7
    • Holmes, K.C.1
  • 34
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • 34. Dominguez, R., Freyzon, Y., Trybus, K.M. & Cohen, C. (1998) Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell 94, 559-571.
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 35
    • 0029960235 scopus 로고    scopus 로고
    • ++-ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Angstrom resolution
    • ++-ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Angstrom resolution. Biochemistry 35, 5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 37
    • 0030768794 scopus 로고    scopus 로고
    • X-ray structures of the MgADP, MgATP-gamma-S, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
    • 37. Gulick, A.M., Bauer, C.B., Thoden, J.B. & Rayment, I. (1997) X-ray structures of the MgADP, MgATP-gamma-S, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry 36, 11619-11628.
    • (1997) Biochemistry , vol.36 , pp. 11619-11628
    • Gulick, A.M.1    Bauer, C.B.2    Thoden, J.B.3    Rayment, I.4
  • 39
    • 0030587932 scopus 로고    scopus 로고
    • An alpha to beta conformational switch in EF-Tu
    • 39. Abel, K., Yoder, M.D., Hilgenfeld, R. & Jurnak, F. (1996) An alpha to beta conformational switch in EF-Tu. Structure 4, 1153-1159.
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 40
    • 15144351296 scopus 로고    scopus 로고
    • Conservation within the myosin motor domain: Implications for structure and function
    • 40. Cope, M., Whisstock, J., Rayment, I. & Kendrick-Jones, J. (1996) Conservation within the myosin motor domain: implications for structure and function. Structure 4, 969-987.
    • (1996) Structure , vol.4 , pp. 969-987
    • Cope, M.1    Whisstock, J.2    Rayment, I.3    Kendrick-Jones, J.4
  • 41
    • 0032499768 scopus 로고    scopus 로고
    • Functional transitions in myosin: Formation of a critical salt bridge and transmission of the effect to the sensitive tryptophan
    • 41. Onishi, H., Kojima, S., Katoh, K., Fujiwara, K., Martinez, H. & Morales, M. (1998) Functional transitions in myosin: formation of a critical salt bridge and transmission of the effect to the sensitive tryptophan. Proc. Natl Acad. Sci. USA 95, 6653-6658.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6653-6658
    • Onishi, H.1    Kojima, S.2    Katoh, K.3    Fujiwara, K.4    Martinez, H.5    Morales, M.6
  • 42
    • 0031848837 scopus 로고    scopus 로고
    • Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing
    • 42. Wriggers, W. & Schulten, K. (1998) Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing. Biophys. J. 75, 646-661.
    • (1998) Biophys. J. , vol.75 , pp. 646-661
    • Wriggers, W.1    Schulten, K.2
  • 43
    • 0029757282 scopus 로고    scopus 로고
    • Binding sites of microtubules of kinesin motors of the same or opposite polarity
    • 43. Song, H. & Endow, S. (1996) Binding sites of microtubules of kinesin motors of the same or opposite polarity. Biochemistry 35, 11203-11209.
    • (1996) Biochemistry , vol.35 , pp. 11203-11209
    • Song, H.1    Endow, S.2
  • 44
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • 44. Hackney, D.D. (1994) Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl Acad. Sci. USA 91, 6865-6869.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 45
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • 45. Ma, Y.Z. & Taylor, E. (1997) Interacting head mechanism of microtubule-kinesin ATPase. J. Biol. Chem. 272, 724-730.
    • (1997) J. Biol. Chem. , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.2
  • 46
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • 46. Gilbert, S.P., Moyer, M.L. & Johnson, K.A. (1998) Alternating site mechanism of the kinesin ATPase. Biochemistry 37, 792-799.
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 47
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • 47. Pai, E., Kabsch, W., Krengel, U., Holmes, K., John, J. & Wittinghofer, A. (1989) Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.1    Kabsch, W.2    Krengel, U.3    Holmes, K.4    John, J.5    Wittinghofer, A.6
  • 48
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
    • 48. Tong, L.A., de Vos, A.M., Milburn, M.V. & Kim, S.H. (1991) Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J. Mol. Biol. 217, 503-516.
    • (1991) J. Mol. Biol. , vol.217 , pp. 503-516
    • Tong, L.A.1    De Vos, A.M.2    Milburn, M.V.3    Kim, S.H.4
  • 49
    • 0028237708 scopus 로고
    • Structural determinants for activation of the alpha-subunit of a heterotrimeric G-protein
    • 49. Lambright, D.G., Noel, J.P., Hamm, H.E. & Sigler, P.B. (1994) Structural determinants for activation of the alpha-subunit of a heterotrimeric G-protein. Nature 369, 621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 50
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-alpha complexed with GTP-gamma-S
    • 50. Noel, J., Hamm, H. & Sigler, P. (1993) The 2.2 Å crystal structure of transducin-alpha complexed with GTP-gamma-S. Nature 366, 654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.1    Hamm, H.2    Sigler, P.3
  • 52
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D, version 2: Photorealistic molecular graphics
    • 52. Merritt, E.A. & Bacon, D.J. (1997) Raster3D, version 2: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.