메뉴 건너뛰기




Volumn 228, Issue 5, 2008, Pages 883-890

Crystal structure analysis of NP24-I: A thaumatin-like protein

Author keywords

Glucanase activity; Antifungal protein; Crystal structure; Thaumatin like protein

Indexed keywords

ANTIFUNGAL AGENT; THAUMATIN PROTEIN, PLANT; VEGETABLE PROTEIN;

EID: 51349117610     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-008-0790-5     Document Type: Article
Times cited : (80)

References (37)
  • 2
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • JD Astwood JN Leach RL Fuchs 1996 Stability of food allergens to digestion in vitro Nat Biotechnol 14 1269 1273
    • (1996) Nat Biotechnol , vol.14 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 3
    • 0030021265 scopus 로고    scopus 로고
    • The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family
    • MA Batalia AF Monzingo S Ernst JD Robertus 1996 The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family Nat Struct Biol 3 19 23
    • (1996) Nat Struct Biol , vol.3 , pp. 19-23
    • Batalia, M.A.1    Monzingo, A.F.2    Ernst, S.3    Robertus, J.D.4
  • 4
    • 2342578126 scopus 로고    scopus 로고
    • Thaumatin-like proteins a new family of pollen and fruit allergens
    • H Breiteneder 2004 Thaumatin-like proteins a new family of pollen and fruit allergens Allergy 59 479 481
    • (2004) Allergy , vol.59 , pp. 479-481
    • Breiteneder, H.1
  • 6
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) Acta Crystallogr D50:760-763
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 8
    • 33747072055 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of NP24-I, an isoform of a thaumatin-like protein from ripe tomato fruits
    • R Ghosh C Chakrabarti 2005 Crystallization and preliminary X-ray diffraction studies of NP24-I, an isoform of a thaumatin-like protein from ripe tomato fruits Acta Crystallogr F61 806 807
    • (2005) Acta Crystallogr , vol.61 , pp. 806-807
    • Ghosh, R.1    Chakrabarti, C.2
  • 9
    • 0033180204 scopus 로고    scopus 로고
    • Some thaumatin-like proteins hydrolyse polymeric β -1, 3-glucans
    • J Grenier C Potvin J Trudel A Asselin 1999 Some thaumatin-like proteins hydrolyse polymeric β -1, 3-glucans Plant J 19 473 480
    • (1999) Plant J , vol.19 , pp. 473-480
    • Grenier, J.1    Potvin, C.2    Trudel, J.3    Asselin, A.4
  • 11
    • 0035116853 scopus 로고    scopus 로고
    • Structure-sweetness relationship in thaumatin: Importance of lysine residues
    • R Kaneko N Kitabatake 2001 Structure-sweetness relationship in thaumatin: importance of lysine residues Chem Senses 26 167 177
    • (2001) Chem Senses , vol.26 , pp. 167-177
    • Kaneko, R.1    Kitabatake, N.2
  • 12
    • 0001519918 scopus 로고
    • A protein induced by NaC1 in suspension cultures of Nicotiana tabacum accumulates in whole plant roots
    • GJ King CE Hussey VA Turner 1986 A protein induced by NaC1 in suspension cultures of Nicotiana tabacum accumulates in whole plant roots Plant Mol Biol 7 441 449
    • (1986) Plant Mol Biol , vol.7 , pp. 441-449
    • King, G.J.1    Hussey, C.E.2    Turner, V.A.3
  • 13
    • 34250109457 scopus 로고
    • Isolation and characterization of a tomato cDNA clone which codes for a salt-induced protein
    • GJ King VA Turner CE Hussey ES Wurtele SM Lee 1988 Isolation and characterization of a tomato cDNA clone which codes for a salt-induced protein Plant Mol Biol 10 401 412
    • (1988) Plant Mol Biol , vol.10 , pp. 401-412
    • King, G.J.1    Turner, V.A.2    Hussey, C.E.3    Wurtele, E.S.4    Lee, S.M.5
  • 14
    • 0000820954 scopus 로고    scopus 로고
    • Environmental and molecular biology of pollen allergens
    • B Knox C Suphioglu 1996 Environmental and molecular biology of pollen allergens Trends Plant Sci 1 156 164
    • (1996) Trends Plant Sci , vol.1 , pp. 156-164
    • Knox, B.1    Suphioglu, C.2
  • 15
    • 0033525649 scopus 로고    scopus 로고
    • Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins
    • H Koiwa H Kato T Nakatsu J Oda Y Yamada F Sato 1999 Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins J Mol Biol 286 1137 1145
    • (1999) J Mol Biol , vol.286 , pp. 1137-1145
    • Koiwa, H.1    Kato, H.2    Nakatsu, T.3    Oda, J.4    Yamada, Y.5    Sato, F.6
  • 19
    • 0038175138 scopus 로고    scopus 로고
    • A molecular basis for the endo-beta 1, 3-glucanase activity of the thaumatin-like proteins from edible fruits
    • L Menu-Bouaouiche C Vriet WJ Peumans A Barre EJ Van Damme P Rougé 2003 A molecular basis for the endo-beta 1, 3-glucanase activity of the thaumatin-like proteins from edible fruits Biochimie 85 123 131
    • (2003) Biochimie , vol.85 , pp. 123-131
    • Menu-Bouaouiche, L.1    Vriet, C.2    Peumans, W.J.3    Barre, A.4    Van Damme, E.J.5    Rougé, P.6
  • 21
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J Navaza 1994 AMoRe: an automated package for molecular replacement Acta Crystallogr A50 157 163
    • (1994) Acta Crystallogr , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A Nicholls KA Sharp B Honig 1991 Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins Struct Funct Genet 11 281 296
    • (1991) Proteins Struct Funct Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 23
    • 0027096460 scopus 로고
    • Crystal structure of a sweet tasting protein thaumatin I, at 1.65 Å resolution
    • CM Ogata PF Gordon AM de Vos SH Kim 1992 Crystal structure of a sweet tasting protein thaumatin I, at 1.65 Å resolution J Mol Biol 228 893 908
    • (1992) J Mol Biol , vol.228 , pp. 893-908
    • Ogata, C.M.1    Gordon, P.F.2    De Vos, A.M.3    Kim, S.H.4
  • 24
    • 0034832178 scopus 로고    scopus 로고
    • Binding interactions between barley thaumatin-like proteins and (1, 3)-β-D-glucans
    • RIW Osmond M Hrmova F Fontaine A Imberty GB Fincher 2001 Binding interactions between barley thaumatin-like proteins and (1, 3)-β-D-glucans Eur J Biochem 268 4190 4199
    • (2001) Eur J Biochem , vol.268 , pp. 4190-4199
    • Osmond, R.I.W.1    Hrmova, M.2    Fontaine, F.3    Imberty, A.4    Fincher, G.B.5
  • 25
    • 0031127606 scopus 로고    scopus 로고
    • Two isoforms of NP24: A thaumatin-like protein in tomato fruit
    • R Pressey 1997 Two isoforms of NP24: a thaumatin-like protein in tomato fruit Phytochemistry 44 1241 1245
    • (1997) Phytochemistry , vol.44 , pp. 1241-1245
    • Pressey, R.1
  • 26
    • 33846631464 scopus 로고    scopus 로고
    • Bioinformatics approaches to classifying allergens and predicting cross-reactivity
    • CH Schein O Ivanciuc W Braun 2007 Bioinformatics approaches to classifying allergens and predicting cross-reactivity Immunol Allergy Clin North Am 27 1 27
    • (2007) Immunol Allergy Clin North Am , vol.27 , pp. 1-27
    • Schein, C.H.1    Ivanciuc, O.2    Braun, W.3
  • 27
    • 84969792040 scopus 로고
    • Molecular cloning of osmotin and regulation of its expression by ABA and adaptation to low water potential
    • NK Singh DE Nelson D Kuhn PM Hasegawa RA Bressan 1989 Molecular cloning of osmotin and regulation of its expression by ABA and adaptation to low water potential Plant Physiol 90 1096 1101
    • (1989) Plant Physiol , vol.90 , pp. 1096-1101
    • Singh, N.K.1    Nelson, D.E.2    Kuhn, D.3    Hasegawa, P.M.4    Bressan, R.A.5
  • 30
    • 1542373564 scopus 로고    scopus 로고
    • Antifungal proteins: Targets, mechanisms and prospective applications
    • T Theis U Stahl 2004 Antifungal proteins: targets, mechanisms and prospective applications Cell Mol Life Sci 61 437 455
    • (2004) Cell Mol Life Sci , vol.61 , pp. 437-455
    • Theis, T.1    Stahl, U.2
  • 31
    • 0032253808 scopus 로고    scopus 로고
    • Several thaumatin-like proteins bind to β-1, 3-glucans
    • J Trudel J Grenier C Potvin A Asselin 1998 Several thaumatin-like proteins bind to β-1, 3-glucans Plant Physiol 118 1431 1438
    • (1998) Plant Physiol , vol.118 , pp. 1431-1438
    • Trudel, J.1    Grenier, J.2    Potvin, C.3    Asselin, A.4
  • 32
    • 0036928978 scopus 로고    scopus 로고
    • Biochemical, molecular and structural analysis of multiple thaumatin-like proteins from the elderberry tree (Sambucus nigra L.)
    • EJM Van Damme D Charels L Menu-Bouaouiche P Proost A Barre P Rougé WJ Peumans 2002 Biochemical, molecular and structural analysis of multiple thaumatin-like proteins from the elderberry tree (Sambucus nigra L.) Planta 214 853 862
    • (2002) Planta , vol.214 , pp. 853-862
    • Van Damme, E.J.M.1    Charels, D.2    Menu-Bouaouiche, L.3    Proost, P.4    Barre, A.5    Rougé, P.6    Peumans, W.J.7
  • 37
    • 0035644196 scopus 로고    scopus 로고
    • Dissection of nucleophilic and acid-base catalysis in glycosidases
    • DL Zechel SG Withers 2001 Dissection of nucleophilic and acid-base catalysis in glycosidases Curr Opin Chem Biol 5 643 649
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 643-649
    • Zechel, D.L.1    Withers, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.