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Volumn 16, Issue 2, 2007, Pages 285-292

The transmembrane homotrimer of ADAM 1 in model lipid bilayers

Author keywords

helical bundles; ADAM 1; Fertilin; Fusion; Homotrimer; Infrared dichroism; Lipid bilayers; Molecular dynamics

Indexed keywords

CARBONYL DERIVATIVE; FERTILIN; HETERODIMER; HYBRID PROTEIN; MEMBRANE PROTEIN; OLIGOMER; PROTEIN ADAM 1; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN;

EID: 33846500705     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062494307     Document Type: Article
Times cited : (5)

References (47)
  • 1
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams, P.D., Arkin, I.T., Engelman, D.M., and Brunger, A.T. 1995. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nat. Struct. Biol. 2: 154-162.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 2
    • 0037064267 scopus 로고    scopus 로고
    • Structural aspects of oligomerization taking place between the transmembrane α-helices of bitopic membrane proteins
    • Arkin, I.T. 2002. Structural aspects of oligomerization taking place between the transmembrane α-helices of bitopic membrane proteins. Biochim. Biophys. Acta 1565: 347-363.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 347-363
    • Arkin, I.T.1
  • 3
    • 0030819982 scopus 로고    scopus 로고
    • Site-directed dichroism as a method for obtaining rotational and orientational constraints for oriented polymers
    • Arkin, I.T., MacKenzie, K.R., and Brunger, A.T. 1997. Site-directed dichroism as a method for obtaining rotational and orientational constraints for oriented polymers. J. Am. Chem. Soc. 119: 8973-8980.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 8973-8980
    • Arkin, I.T.1    MacKenzie, K.R.2    Brunger, A.T.3
  • 4
    • 0043272529 scopus 로고    scopus 로고
    • Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)
    • Becherer, J.D. and Blobel, C.P. 2003. Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs). Curr. Top. Dev. Biol. 54: 101-123.
    • (2003) Curr. Top. Dev. Biol , vol.54 , pp. 101-123
    • Becherer, J.D.1    Blobel, C.P.2
  • 5
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence
    • Blobel, C.P., Myles, D.G., Primakoff, P., and White, J.M. 1990. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111: 69-78.
    • (1990) J. Cell Biol , vol.111 , pp. 69-78
    • Blobel, C.P.1    Myles, D.G.2    Primakoff, P.3    White, J.M.4
  • 6
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P., Wolfsberg, T.G., Turck, C.W., Myles, D.G., Primakoff, P., and White, J.M. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356: 248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 7
    • 33744782354 scopus 로고    scopus 로고
    • Conformation of the synaptobrevin transmembrane domain
    • Bowen, M. and Brunger, A.T. 2006. Conformation of the synaptobrevin transmembrane domain. Proc. Natl. Acad. Sci. 103: 8378-8383.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 8378-8383
    • Bowen, M.1    Brunger, A.T.2
  • 8
    • 0035882546 scopus 로고    scopus 로고
    • A new method to model membrane protein structure based on silent amino acid substitutions
    • Briggs, J.A.G., Torres, J., and Arkin, I.T. 2001. A new method to model membrane protein structure based on silent amino acid substitutions. Proteins 44: 370-375.
    • (2001) Proteins , vol.44 , pp. 370-375
    • Briggs, J.A.G.1    Torres, J.2    Arkin, I.T.3
  • 10
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D.M. and Susi, H. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25: 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 12
    • 0034660644 scopus 로고    scopus 로고
    • Analysis of mouse fertilin in wild-type and fertilin β(-/-) sperm: Evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin α in sperm-egg fusion
    • Cho, C., Ge, H., Branciforte, D., Primakoff, P., and Myles, D.G. 2000. Analysis of mouse fertilin in wild-type and fertilin β(-/-) sperm: Evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin α in sperm-egg fusion. Dev. Biol. 222: 289-295.
    • (2000) Dev. Biol , vol.222 , pp. 289-295
    • Cho, C.1    Ge, H.2    Branciforte, D.3    Primakoff, P.4    Myles, D.G.5
  • 13
    • 0035881954 scopus 로고    scopus 로고
    • Guinea pig fertilin exhibits restricted lateral mobility in epididymal sperm and becomes freely diffusing during capacitation
    • Cowan, A.E., Koppel, D.E., Vargas, L.A., and Hunnicutt, G.R. 2001. Guinea pig fertilin exhibits restricted lateral mobility in epididymal sperm and becomes freely diffusing during capacitation. Dev. Biol. 236: 502-509.
    • (2001) Dev. Biol , vol.236 , pp. 502-509
    • Cowan, A.E.1    Koppel, D.E.2    Vargas, L.A.3    Hunnicutt, G.R.4
  • 14
    • 32544454232 scopus 로고    scopus 로고
    • Exploiting common targets in human fertilization and HIV infection: Development of novel contraceptive microbicides
    • Doncel, G.F. 2006. Exploiting common targets in human fertilization and HIV infection: Development of novel contraceptive microbicides. Hum. Reprod. Update 12: 103-117.
    • (2006) Hum. Reprod. Update , vol.12 , pp. 103-117
    • Doncel, G.F.1
  • 16
    • 0031282203 scopus 로고    scopus 로고
    • Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis
    • Hunnicutt, G.R., Koppel, D.E., and Myles, D.G. 1997. Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis. Dev. Biol. 191: 146-159.
    • (1997) Dev. Biol , vol.191 , pp. 146-159
    • Hunnicutt, G.R.1    Koppel, D.E.2    Myles, D.G.3
  • 17
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • Inoue, N., Ikawa, M., Isotani, A., and Okabe, M. 2005. The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434: 234-238.
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 18
    • 13444281378 scopus 로고    scopus 로고
    • Synthesis, processing, and subcellular localization of mouse ADAM3 during spermatogenesis and epididymal sperm transport
    • Kim, E., Nishimura, H., Iwase, S., Yamagata, K., Kashiwabara, S.-I., and Baba, T. 2004. Synthesis, processing, and subcellular localization of mouse ADAM3 during spermatogenesis and epididymal sperm transport. J. Reprod. Dev. 50: 571-578.
    • (2004) J. Reprod. Dev , vol.50 , pp. 571-578
    • Kim, E.1    Nishimura, H.2    Iwase, S.3    Yamagata, K.4    Kashiwabara, S.-I.5    Baba, T.6
  • 19
    • 33646838999 scopus 로고    scopus 로고
    • Mouse sperm lacking ADAM1b/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization
    • Kim, E., Yamashita, M., Nakanishi, T., Park, K.E., Kimura, M., Kashiwabara, S., and Baba, T. 2006. Mouse sperm lacking ADAM1b/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization. J. Biol. Chem. 281: 5634-5639.
    • (2006) J. Biol. Chem , vol.281 , pp. 5634-5639
    • Kim, E.1    Yamashita, M.2    Nakanishi, T.3    Park, K.E.4    Kimura, M.5    Kashiwabara, S.6    Baba, T.7
  • 20
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E.L.L. 2001. Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305: 567-580.
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.L.4
  • 21
    • 0033605318 scopus 로고    scopus 로고
    • Experimentally based orientational refinement of membrane protein models: A structure for the Influenza A M2 H+ channel
    • Kukol, A., Adams, P.D., Rice, L.M., Brunger, A.T., and Arkin, T.I. 1999. Experimentally based orientational refinement of membrane protein models: A structure for the Influenza A M2 H+ channel. J. Mol. Biol. 286: 951-962.
    • (1999) J. Mol. Biol , vol.286 , pp. 951-962
    • Kukol, A.1    Adams, P.D.2    Rice, L.M.3    Brunger, A.T.4    Arkin, T.I.5
  • 23
    • 0032387628 scopus 로고    scopus 로고
    • Structural properties of the putative fusion peptide of fertilin, a protein active in sperm-egg fusion, upon interaction with the lipid bilayer
    • Martin, I., Epand, R.M., and Ruysschaert, J.M. 1998. Structural properties of the putative fusion peptide of fertilin, a protein active in sperm-egg fusion, upon interaction with the lipid bilayer. Biochemistry 37: 17030-17039.
    • (1998) Biochemistry , vol.37 , pp. 17030-17039
    • Martin, I.1    Epand, R.M.2    Ruysschaert, J.M.3
  • 24
    • 0035909077 scopus 로고    scopus 로고
    • Retention of native-like oligomerization states in transmembrane segment peptides: Application to the Escherichia coli aspartate receptor
    • Melnyk, R.A., Partridge, A.W., and Deber, C.M. 2001. Retention of native-like oligomerization states in transmembrane segment peptides: Application to the Escherichia coli aspartate receptor. Biochemistry 40: 11106-11113.
    • (2001) Biochemistry , vol.40 , pp. 11106-11113
    • Melnyk, R.A.1    Partridge, A.W.2    Deber, C.M.3
  • 25
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga, A., Neugebauer, W., Hirama, T., and Surewicz, W.K. 1994. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry 33: 4444-4448.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 26
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface
    • Nishimura, H., Kim, E., Nakanishi, T., and Baba, T. 2004. Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface. J. Biol. Chem. 279: 34957-34962.
    • (2004) J. Biol. Chem , vol.279 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 27
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff, P. and Myles, D.G. 2000. The ADAM gene family: Surface proteins with adhesion and protease activity. Trends Genet. 16: 83-87.
    • (2000) Trends Genet , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 28
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • Primakoff, P., Hyatt, H., and Tredick-Kline, J. 1987. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104: 141-149.
    • (1987) J. Cell Biol , vol.104 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 30
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J.J. and Wiley, D.C. 2000. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu. Rev. Biochem. 69: 531-569.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 31
    • 2442629758 scopus 로고    scopus 로고
    • Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation
    • Swalley, S.E., Baker, B.M., Calder, L.J., Harrison, S.C., Skehel, J.J., and Wiley, D.C. 2004. Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation. Biochemistry 43: 5902-5911.
    • (2004) Biochemistry , vol.43 , pp. 5902-5911
    • Swalley, S.E.1    Baker, B.M.2    Calder, L.J.3    Harrison, S.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 32
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm, L.K. and Tatulian, S.A. 1997. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30: 365-429.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 33
    • 0034711760 scopus 로고    scopus 로고
    • Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin
    • Tatulian, S.A. and Tamm, L.K. 2000. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin. Biochemistry 39: 496-507.
    • (2000) Biochemistry , vol.39 , pp. 496-507
    • Tatulian, S.A.1    Tamm, L.K.2
  • 34
    • 0034697895 scopus 로고    scopus 로고
    • 18O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data
    • 18O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data. J. Mol. Biol. 300: 677-685.
    • (2000) J. Mol. Biol , vol.300 , pp. 677-685
    • Torres, J.1    Adams, P.D.2    Arkin, I.T.3
  • 35
    • 0033636640 scopus 로고    scopus 로고
    • Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy
    • Torres, J., Kukol, A., and Arkin, I.T. 2000b. Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy. Biophys. J. 79: 3139-3143.
    • (2000) Biophys. J , vol.79 , pp. 3139-3143
    • Torres, J.1    Kukol, A.2    Arkin, I.T.3
  • 36
    • 0036293994 scopus 로고    scopus 로고
    • Multiple site-specific infrared dichroism of CD3-ζ, a transmembrane helix bundle
    • Torres, J., Briggs, J.A., and Arkin, I.T. 2002. Multiple site-specific infrared dichroism of CD3-ζ, a transmembrane helix bundle. J. Mol. Biol. 316: 365-374.
    • (2002) J. Mol. Biol , vol.316 , pp. 365-374
    • Torres, J.1    Briggs, J.A.2    Arkin, I.T.3
  • 37
    • 21244448326 scopus 로고    scopus 로고
    • The transmembrane oligomers of coronavirus protein E
    • Torres, J., Wang, J., Parthasarathy, K., and Liu, D.X. 2005. The transmembrane oligomers of coronavirus protein E. Biophys. J. 88: 1283-1290.
    • (2005) Biophys. J , vol.88 , pp. 1283-1290
    • Torres, J.1    Wang, J.2    Parthasarathy, K.3    Liu, D.X.4
  • 38
    • 0001242101 scopus 로고
    • Infrared dichroism and molecular conformation of α-form poly-g-benzyl-L-glutamate
    • Tsuboi, M. 1962. Infrared dichroism and molecular conformation of α-form poly-g-benzyl-L-glutamate. J. Polym. Sci. [B] 59: 139-153.
    • (1962) J. Polym. Sci. [B] , vol.59 , pp. 139-153
    • Tsuboi, M.1
  • 39
    • 0030940446 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex
    • Waters, S.I. and White, J.M. 1997. Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex. Biol. Reprod. 56: 1245-1254.
    • (1997) Biol. Reprod , vol.56 , pp. 1245-1254
    • Waters, S.I.1    White, J.M.2
  • 42
    • 0032849530 scopus 로고    scopus 로고
    • Membrane interactions of the putative fusion peptide (MFαP) from fertilin-α, the mouse sperm protein complex involved in fertilization
    • Wolfe, C.A., Cladera, J., Ladha, S., Senior, S., Jones, R., and O'Shea, P. 1999. Membrane interactions of the putative fusion peptide (MFαP) from fertilin-α, the mouse sperm protein complex involved in fertilization. Mol. Membr. Biol. 16: 257-263.
    • (1999) Mol. Membr. Biol , vol.16 , pp. 257-263
    • Wolfe, C.A.1    Cladera, J.2    Ladha, S.3    Senior, S.4    Jones, R.5    O'Shea, P.6
  • 43
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • Wolfsberg, T.G. and White, J.M. 1996. ADAMs in fertilization and development. Dev. Biol. 180: 389-401.
    • (1996) Dev. Biol , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2
  • 44
    • 0027431501 scopus 로고
    • The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: Structural, functional, and evolutionary implications
    • Wolfsberg, T.G., Bazan, J.F., Blobel, C.P., Myles, D.G., Primakoff, P., and White, J.M. 1993. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: Structural, functional, and evolutionary implications. Proc. Natl. Acad. Sci. 90: 10783-10787.
    • (1993) Proc. Natl. Acad. Sci , vol.90 , pp. 10783-10787
    • Wolfsberg, T.G.1    Bazan, J.F.2    Blobel, C.P.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 45
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg, T.G., Straight, P.D., Gerena, R.L., Huovila, A.P., Primakoff, P., Myles, D.G., and White, J.M. 1995. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev. Biol. 169: 378-383.
    • (1995) Dev. Biol , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.P.4    Primakoff, P.5    Myles, D.G.6    White, J.M.7
  • 46
    • 0035816640 scopus 로고    scopus 로고
    • Analysis of fertilin alpha (ADAM1)-mediated sperm-egg cell adhesion during fertilization and identification of an adhesion-mediating sequence in the disintegrin-like domain
    • Wong, G.E., Zhu, X., Prater, C.E., Oh, E., and Evans, J.P. 2001. Analysis of fertilin alpha (ADAM1)-mediated sperm-egg cell adhesion during fertilization and identification of an adhesion-mediating sequence in the disintegrin-like domain. J. Biol. Chem. 276: 24937-24945.
    • (2001) J. Biol. Chem , vol.276 , pp. 24937-24945
    • Wong, G.E.1    Zhu, X.2    Prater, C.E.3    Oh, E.4    Evans, J.P.5
  • 47
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt, R. and Sodroski, J. 1998. The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens. Science 280: 1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2


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