메뉴 건너뛰기




Volumn 1784, Issue 4, 2008, Pages 651-657

Deswapping bovine odorant binding protein

Author keywords

Crystal structure; Domain swapping; Odorant binding protein; Olfaction

Indexed keywords

1 AMINO ANTHRACENE; 1 OCTEN 3 OL; ANTHRACENE; BINDING PROTEIN; BOVINE ODORANT BINDING PROTEIN; CYSTEINE; DISULFIDE; HISTIDINE; LIGAND; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 40849097846     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.01.010     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: structure and function
    • Flower D.R. The lipocalin protein family: structure and function. Biochem J. 318 Pt 1 (1996) 1-14
    • (1996) Biochem J. , vol.318 , Issue.PART 1 , pp. 1-14
    • Flower, D.R.1
  • 2
    • 0034684227 scopus 로고    scopus 로고
    • Experimentally determined lipocalin structures
    • Flower D.R. Experimentally determined lipocalin structures. Biochim. Biophys. Acta 1482 (2000) 46-56
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 46-56
    • Flower, D.R.1
  • 3
    • 33644506112 scopus 로고    scopus 로고
    • Comparative ligand-binding analysis of ten human lipocalins
    • Breustedt D.A., Schonfeld D.L., and Skerra A. Comparative ligand-binding analysis of ten human lipocalins. Biochim. Biophys. Acta 1764 (2006) 161-173
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 161-173
    • Breustedt, D.A.1    Schonfeld, D.L.2    Skerra, A.3
  • 5
    • 0035033499 scopus 로고    scopus 로고
    • The role of perireceptor events in vertebrate olfaction
    • Pelosi P. The role of perireceptor events in vertebrate olfaction. Cell. Mol. Life Sci. 58 (2001) 503-509
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 503-509
    • Pelosi, P.1
  • 6
    • 0037062575 scopus 로고    scopus 로고
    • Evidence of an odorant-binding protein in the human olfactory mucus: location, structural characterization, and odorant-binding properties
    • Briand L., Eloit C., Nespoulous C., Bezirard V., Huet J.C., Henry C., Blon F., Trotier D., and Pernollet J.C. Evidence of an odorant-binding protein in the human olfactory mucus: location, structural characterization, and odorant-binding properties. Biochemistry 41 (2002) 7241-7252
    • (2002) Biochemistry , vol.41 , pp. 7241-7252
    • Briand, L.1    Eloit, C.2    Nespoulous, C.3    Bezirard, V.4    Huet, J.C.5    Henry, C.6    Blon, F.7    Trotier, D.8    Pernollet, J.C.9
  • 7
    • 2342508009 scopus 로고    scopus 로고
    • Pheromone-binding proteins contribute to the activation of olfactory receptor neurons in the silkmoths Antheraea polyphemus and Bombyx mori
    • Pophof B. Pheromone-binding proteins contribute to the activation of olfactory receptor neurons in the silkmoths Antheraea polyphemus and Bombyx mori. Chem. Senses 29 (2004) 117-125
    • (2004) Chem. Senses , vol.29 , pp. 117-125
    • Pophof, B.1
  • 8
    • 12344262334 scopus 로고    scopus 로고
    • Drosophila OBP LUSH is required for activity of pheromone-sensitive neurons
    • Xu P., Atkinson R., Jones D.N., and Smith D.P. Drosophila OBP LUSH is required for activity of pheromone-sensitive neurons. Neuron 45 (2005) 193-200
    • (2005) Neuron , vol.45 , pp. 193-200
    • Xu, P.1    Atkinson, R.2    Jones, D.N.3    Smith, D.P.4
  • 9
    • 34249011110 scopus 로고    scopus 로고
    • Odorant-binding proteins OBP57d and OBP57e affect taste perception and host-plant preference in Drosophila sechellia
    • Matsuo T., Sugaya S., Yasukawa J., Aigaki T., and Fuyama Y. Odorant-binding proteins OBP57d and OBP57e affect taste perception and host-plant preference in Drosophila sechellia. PLoS Biol. 5 (2007) e118
    • (2007) PLoS Biol. , vol.5
    • Matsuo, T.1    Sugaya, S.2    Yasukawa, J.3    Aigaki, T.4    Fuyama, Y.5
  • 10
    • 0034733389 scopus 로고    scopus 로고
    • Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes
    • Vincent F., Spinelli S., Ramoni R., Grolli S., Pelosi P., Cambillau C., and Tegoni M. Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes. J. Mol. Biol. 300 (2000) 127-139
    • (2000) J. Mol. Biol. , vol.300 , pp. 127-139
    • Vincent, F.1    Spinelli, S.2    Ramoni, R.3    Grolli, S.4    Pelosi, P.5    Cambillau, C.6    Tegoni, M.7
  • 11
    • 4944250096 scopus 로고    scopus 로고
    • Crystal structures of bovine odorant-binding protein in complex with odorant molecules
    • Vincent F., Ramoni R., Spinelli S., Grolli S., Tegoni M., and Cambillau C. Crystal structures of bovine odorant-binding protein in complex with odorant molecules. Eur. J. Biochem. 271 (2004) 3832-3842
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3832-3842
    • Vincent, F.1    Ramoni, R.2    Spinelli, S.3    Grolli, S.4    Tegoni, M.5    Cambillau, C.6
  • 12
    • 0034109042 scopus 로고    scopus 로고
    • Ligand-binding properties and structural characterization of a novel rat odorant-binding protein variant
    • Briand L., Nespoulous C., Perez V., Remy J.J., Huet J.C., and Pernollet J.C. Ligand-binding properties and structural characterization of a novel rat odorant-binding protein variant. Eur. J. Biochem. 267 (2000) 3079-3089
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3079-3089
    • Briand, L.1    Nespoulous, C.2    Perez, V.3    Remy, J.J.4    Huet, J.C.5    Pernollet, J.C.6
  • 13
    • 0036200906 scopus 로고    scopus 로고
    • Odorants of different chemical classes interact with distinct odorant binding protein subtypes
    • Lobel D., Jacob M., Volkner M., and Breer H. Odorants of different chemical classes interact with distinct odorant binding protein subtypes. Chem. Senses 27 (2002) 39-44
    • (2002) Chem. Senses , vol.27 , pp. 39-44
    • Lobel, D.1    Jacob, M.2    Volkner, M.3    Breer, H.4
  • 14
    • 0032474475 scopus 로고    scopus 로고
    • The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism
    • Spinelli S., Ramoni R., Grolli S., Bonicel J., Cambillau C., and Tegoni M. The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry 37 (1998) 7913-7918
    • (1998) Biochemistry , vol.37 , pp. 7913-7918
    • Spinelli, S.1    Ramoni, R.2    Grolli, S.3    Bonicel, J.4    Cambillau, C.5    Tegoni, M.6
  • 15
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
    • Tegoni M., Ramoni R., Bignetti E., Spinelli S., and Cambillau C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nat. Struct. Biol. 3 (1996) 863-867
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 863-867
    • Tegoni, M.1    Ramoni, R.2    Bignetti, E.3    Spinelli, S.4    Cambillau, C.5
  • 18
    • 0025259871 scopus 로고
    • Odorant-binding protein. Characterization of ligand binding
    • Pevsner J., Hou V., Snowman A.M., and Snyder S.H. Odorant-binding protein. Characterization of ligand binding. J. Biol. Chem. 265 (1990) 6118-6125
    • (1990) J. Biol. Chem. , vol.265 , pp. 6118-6125
    • Pevsner, J.1    Hou, V.2    Snowman, A.M.3    Snyder, S.H.4
  • 21
    • 0032932846 scopus 로고    scopus 로고
    • Porcine odorant-binding protein: structural stability and ligand affinities measured by fourier-transform infrared spectroscopy and fluorescence spectroscopy
    • Paolini S., Tanfani F., Fini C., Bertoli E., and Pelosi P. Porcine odorant-binding protein: structural stability and ligand affinities measured by fourier-transform infrared spectroscopy and fluorescence spectroscopy. Biochim. Biophys. Acta 1431 (1999) 179-188
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 179-188
    • Paolini, S.1    Tanfani, F.2    Fini, C.3    Bertoli, E.4    Pelosi, P.5
  • 22
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 24
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for crystallography
    • CCP4 and C.C.P.N. 4. The CCP4 suite: programs for crystallography. Acta Cryst. D 50 (1994) 760-766
    • (1994) Acta Cryst. , vol.D 50 , pp. 760-766
    • CCP4 and C.C.P.N. 41
  • 25
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50 (1994) 157-163
    • (1994) Acta Crystallog. sect. A. , vol.50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. , vol.D 53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.A.2    Dodson, E.J.3
  • 27
    • 2142788231 scopus 로고
    • Silicon graphics Geometry Partners Directory, Mountain View, USA
    • Roussel A., and Cambillau C. The TURBO-FRODO graphics package vol. 81 (1991), Silicon graphics Geometry Partners Directory, Mountain View, USA
    • (1991) The TURBO-FRODO graphics package , vol.81
    • Roussel, A.1    Cambillau, C.2
  • 28
    • 0001513485 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R., MacArthur M., Moss D., and Thornton J. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 91-97
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 91-97
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 29
    • 0036113683 scopus 로고    scopus 로고
    • Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/androstenone docking simulations
    • Spinelli S., Vincent F., Pelosi P., Tegoni M., and Cambillau C. Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/androstenone docking simulations. Eur. J. Biochem. 269 (2002) 2449-2456
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2449-2456
    • Spinelli, S.1    Vincent, F.2    Pelosi, P.3    Tegoni, M.4    Cambillau, C.5
  • 31
    • 1042278146 scopus 로고    scopus 로고
    • Sulfur single-wavelength anomalous diffraction crystal structure of a pheromone-binding protein from the honeybee Apis mellifera L
    • Lartigue A., Gruez A., Briand L., Blon F., Bezirard V., Walsh M., Pernollet J.C., Tegoni M., and Cambillau C. Sulfur single-wavelength anomalous diffraction crystal structure of a pheromone-binding protein from the honeybee Apis mellifera L. J. Biol. Chem. 279 (2004) 4459-4464
    • (2004) J. Biol. Chem. , vol.279 , pp. 4459-4464
    • Lartigue, A.1    Gruez, A.2    Briand, L.3    Blon, F.4    Bezirard, V.5    Walsh, M.6    Pernollet, J.C.7    Tegoni, M.8    Cambillau, C.9
  • 32
    • 0028865843 scopus 로고
    • 3D domain swapping: a mechanism for oligomer assembly
    • Bennett M.J., Schlunegger M.P., and Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4 (1995) 2455-2468
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 33
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly
    • Schlunegger M.P., Bennett M.J., and Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50 (1997) 61-122
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 34
    • 4143058003 scopus 로고    scopus 로고
    • The evolving role of 3D domain swapping in proteins
    • Bennett M.J., and Eisenberg D. The evolving role of 3D domain swapping in proteins. Structure 12 (2004) 1339-1341
    • (2004) Structure , vol.12 , pp. 1339-1341
    • Bennett, M.J.1    Eisenberg, D.2
  • 35
  • 36
    • 33646375442 scopus 로고    scopus 로고
    • Deposition diseases and 3D domain swapping
    • Bennett M.J., Sawaya M.R., and Eisenberg D. Deposition diseases and 3D domain swapping. Structure 14 (2006) 811-824
    • (2006) Structure , vol.14 , pp. 811-824
    • Bennett, M.J.1    Sawaya, M.R.2    Eisenberg, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.