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Volumn 6, Issue 10, 1998, Pages 1245-1254

Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction

Author keywords

Crystal structure; Hippocampal neurostimulatory peptide precursor; Phosphatidylethanolamine binding protein; Signalling

Indexed keywords

ANIMALIA; MAGNOLIOPHYTA;

EID: 0032532458     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00125-7     Document Type: Article
Times cited : (186)

References (35)
  • 1
    • 0029123401 scopus 로고
    • From structure to function: Possible biological roles of a new widespread protein family binding Hydrophobic ligands and displaying a nucleotide binding site
    • Schoentgen, F. & Jolles, P. (1995). From structure to function: possible biological roles of a new widespread protein family binding Hydrophobic ligands and displaying a nucleotide binding site. FEBS Lett. 369, 22-26.
    • (1995) FEBS Lett. , vol.369 , pp. 22-26
    • Schoentgen, F.1    Jolles, P.2
  • 2
    • 0021751250 scopus 로고
    • Purification and characterisation of a basic 23 kDa cytosolic protein from bovine brain
    • Bernier, I. & Jolles, P. (1984). Purification and characterisation of a basic 23 kDa cytosolic protein from bovine brain. Biochim. Biophys. Acta 790, 174-181.
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 174-181
    • Bernier, I.1    Jolles, P.2
  • 3
    • 0022445734 scopus 로고
    • Ligand-binding studies with a 23-kDa protein purified from bovine brain cytosol
    • Bernier, I., Tresca, J.P. & Jolles, P. (1986). Ligand-binding studies with a 23-kDa protein purified from bovine brain cytosol. Biochim. Biophys. Acta 871, 19-23.
    • (1986) Biochim. Biophys. Acta , vol.871 , pp. 19-23
    • Bernier, I.1    Tresca, J.P.2    Jolles, P.3
  • 4
    • 0023910383 scopus 로고    scopus 로고
    • 3 in subsets of tissues from different species
    • 3 in subsets of tissues from different species. J. Neurochem. 50, 1210-1214.
    • (1998) J. Neurochem. , vol.50 , pp. 1210-1214
    • Bollengier, F.1    Mahler, A.2
  • 5
    • 0023655581 scopus 로고
    • Complete amino acid sequence of a basic 21 kDa protein from bovine brain cytosol
    • Schoentgen, F., Saccoccio, F., Jolles, J., Bernier, I. & Jolies, P. (1987). Complete amino acid sequence of a basic 21 kDa protein from bovine brain cytosol. Eur. J. Biochem. 166, 333-338.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 333-338
    • Schoentgen, F.1    Saccoccio, F.2    Jolles, J.3    Bernier, I.4    Jolies, P.5
  • 6
    • 0028352920 scopus 로고
    • Sequence analysis of a mammalian phospholipid-binding protein from testis and epididymis and its distribution between spermatozoa and extracellular secretions
    • Perry, A.C.F., Hall, L., Bell, A.E. & Jones, R. (1994). Sequence analysis of a mammalian phospholipid-binding protein from testis and epididymis and its distribution between spermatozoa and extracellular secretions. Biochem. J. 301, 235-242.
    • (1994) Biochem. J. , vol.301 , pp. 235-242
    • Perry, A.C.F.1    Hall, L.2    Bell, A.E.3    Jones, R.4
  • 7
    • 0026758157 scopus 로고
    • Isolation and characterization of a 25 kilodalton protein from mouse testis: Sequence homology with a phospholipid-binding protein
    • Araki, Y., Vierula, M.E., Rankin, T.L., Tulsiani, D.R. & Orgebin-Crist, M.-C. (1992). Isolation and characterization of a 25 kilodalton protein from mouse testis: sequence homology with a phospholipid-binding protein. Biol. Reprod. 47, 832-843.
    • (1992) Biol. Reprod. , vol.47 , pp. 832-843
    • Araki, Y.1    Vierula, M.E.2    Rankin, T.L.3    Tulsiani, D.R.4    Orgebin-Crist, M.-C.5
  • 8
    • 0028123735 scopus 로고
    • Members of a family of Drosophila putative odorant-binding proteins are expressed in different subsets of olfactory hairs
    • Pikielny, C.W., Hasan, G., Rouyer, F. & Rosbash, M. (1994). Members of a family of Drosophila putative odorant-binding proteins are expressed in different subsets of olfactory hairs. Neuron 12, 35-49.
    • (1994) Neuron , vol.12 , pp. 35-49
    • Pikielny, C.W.1    Hasan, G.2    Rouyer, F.3    Rosbash, M.4
  • 9
    • 0026038613 scopus 로고
    • TFS1 - A suppressor of CDC25 mutations in Saccharomyces cerevisiae
    • Bobinson, L.C. & Tatchell, K. (1991). TFS1 - a suppressor of CDC25 mutations in Saccharomyces cerevisiae. Mol. Gen. Genet. 230, 241-250.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 241-250
    • Bobinson, L.C.1    Tatchell, K.2
  • 10
    • 0028964574 scopus 로고
    • The primary structure of a putative phosphatidylethanolamine-binding protein from Plasmodium falciparum
    • Trottein, F. & Cowman, A.F. (1995). The primary structure of a putative phosphatidylethanolamine-binding protein from Plasmodium falciparum. Mol. Biochem. Parasitol. 70, 235-239.
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 235-239
    • Trottein, F.1    Cowman, A.F.2
  • 11
    • 0029799708 scopus 로고    scopus 로고
    • Onchocerca volvulus: Identification of cDNAs encoding a putative phosphatidylethanolamine-binding protein and a putative partially processed mRNA precursor
    • Erttmann, K.D. & Galin, M.Y. (1996). Onchocerca volvulus: identification of cDNAs encoding a putative phosphatidylethanolamine-binding protein and a putative partially processed mRNA precursor. Gene 174, 203-207.
    • (1996) Gene , vol.174 , pp. 203-207
    • Erttmann, K.D.1    Galin, M.Y.2
  • 12
    • 0029150195 scopus 로고
    • An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26 kDa protein with homology to phosphatidylethanolamine-binding proteins
    • Gems, D., et al., & Maizels, R.M. (1995). An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26 kDa protein with homology to phosphatidylethanolamine-binding proteins. J. Biol. Chem. 270, 18517-18522.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18517-18522
    • Gems, D.1    Maizels, R.M.2
  • 14
    • 0030889655 scopus 로고    scopus 로고
    • Cloning and molecular analysis of the Arabidopsis gene Terminal Flower 1
    • Ohshima, S., Murata, M., Sakamoto, W., Ogura, Y. & Motoyoshi, F. (1997). Cloning and molecular analysis of the Arabidopsis gene Terminal Flower 1. Mol. Gen. Genet. 254, 186-194.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 186-194
    • Ohshima, S.1    Murata, M.2    Sakamoto, W.3    Ogura, Y.4    Motoyoshi, F.5
  • 15
    • 0028113952 scopus 로고
    • 3), comparison with its counterparts from Rattus norvegicus ans Bos taurus, and expression of its messenger RNA in different tissues
    • 3), comparison with its counterparts from Rattus norvegicus ans Bos taurus, and expression of its messenger RNA in different tissues. J. Mol. Evol. 39, 655-660.
    • (1994) J. Mol. Evol. , vol.39 , pp. 655-660
    • Seddiqi, N.1    Schoentgen, F.2
  • 16
  • 17
    • 0028104165 scopus 로고
    • Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21 -kDa protein
    • Bucquoy, S., Jollés, P. & Schoentgen, F. (1994). Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21 -kDa protein. Eur. J. Biochem. 225, 1203-1210.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1203-1210
    • Bucquoy, S.1    Jollés, P.2    Schoentgen, F.3
  • 18
    • 0029069889 scopus 로고
    • Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein
    • Tohdoh, N., Tojo, S., Agui, H. & Ojika, K. (1995). Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein. Mol. Brain Res. 30, 381-384.
    • (1995) Mol. Brain Res. , vol.30 , pp. 381-384
    • Tohdoh, N.1    Tojo, S.2    Agui, H.3    Ojika, K.4
  • 19
    • 0031127063 scopus 로고    scopus 로고
    • Mechanism of expression of the rat HCNP precursor protein gene
    • Tohdoh, N., Tojo, S., Kimura, M., Ishii, T. & Ojika, K. (1997). Mechanism of expression of the rat HCNP precursor protein gene. Mol. Brain Res. 45, 24-32.
    • (1997) Mol. Brain Res. , vol.45 , pp. 24-32
    • Tohdoh, N.1    Tojo, S.2    Kimura, M.3    Ishii, T.4    Ojika, K.5
  • 20
    • 0026689451 scopus 로고
    • Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated through hydrophobic cluster analysis and molecular modelling
    • Schoentgen, F., et al., & Mornon, J.-P. (1992). Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated through hydrophobic cluster analysis and molecular modelling. Protein Eng. 5, 295-303.
    • (1992) Protein Eng. , vol.5 , pp. 295-303
    • Schoentgen, F.1    Mornon, J.-P.2
  • 21
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 223, 123-138.
    • (1993) J. Mol. Biol. , vol.223 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 24
    • 0026055156 scopus 로고
    • Analysis of the strike strain in the polypeptide backbone of protein molecules
    • Herzberg, O. & Moult, J. (1991). Analysis of the strike strain in the polypeptide backbone of protein molecules. Proteins 11, 223-229.
    • (1991) Proteins , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 25
    • 0026206788 scopus 로고
    • Sparse-matrix sampling - A screening method for crystallisation of proteins
    • Jancarik, J. & Kim, S.H. (1991). Sparse-matrix sampling - a screening method for crystallisation of proteins. J. Appl. Cryst. 24, 409-411.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Carter, C.W. Jr & Sweet, R.M., eds), Academic press, New York
    • Otwinoski, Z. & Minor, W. (1996). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology. (Carter, C.W. Jr & Sweet, R.M., eds), Vol. 276, pp. 307-326, Academic press, New York.
    • (1996) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein structures in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein structures in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 31
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt, G.J. & Jones, T.A. (1996). Phi/psi-chology: Ramachandran revisited. Structure 4, 1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt, E.A. & Bacon, D.J. (1997). Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 34
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. (1988). Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16, 10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 35
    • 0026319199 scopus 로고
    • Protein folding and association - Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-196.
    • (1991) Proteins , vol.11 , pp. 281-1196
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.