메뉴 건너뛰기




Volumn 401, Issue 1, 2010, Pages 68-83

Crystal Structure of the Dog Lipocalin Allergen Can f 2: Implications for Cross-reactivity to the Cat Allergen Fel d 4

Author keywords

Crystal structure; Dog allergen; Epitope; Lipocalin fold; Recombinant Can f 2

Indexed keywords

ALLERGEN FEL D 4; IMMUNOGLOBULIN E; LIPOCALIN; LIPOCALIN ALLERGEN CAN F 2; RECOMBINANT ALLERGEN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 77954761516     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.05.043     Document Type: Article
Times cited : (56)

References (73)
  • 1
    • 0027199999 scopus 로고
    • Allergens in school dust. I. The amount of the major cat (Fel d I) and dog (Can f I) allergens in dust from Swedish schools is high enough to probably cause perennial symptoms in most children with asthma who are sensitized to cat and dog
    • Munir A.K., Einarsson R., Schou C., Dreborg S.K. Allergens in school dust. I. The amount of the major cat (Fel d I) and dog (Can f I) allergens in dust from Swedish schools is high enough to probably cause perennial symptoms in most children with asthma who are sensitized to cat and dog. J. Allergy Clin. Immunol. 1993, 91:1067-1074.
    • (1993) J. Allergy Clin. Immunol. , vol.91 , pp. 1067-1074
    • Munir, A.K.1    Einarsson, R.2    Schou, C.3    Dreborg, S.K.4
  • 3
    • 33646466339 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic data of a Fel d 1 (1+2) construct corresponding to the major allergen from cat
    • Kaiser L., Grönlund H., van Hage-Hamsten M., Achour A. Crystallization and preliminary crystallographic data of a Fel d 1 (1+2) construct corresponding to the major allergen from cat. Acta Crystallogr. F 2005, 61:232-234.
    • (2005) Acta Crystallogr. F , vol.61 , pp. 232-234
    • Kaiser, L.1    Grönlund, H.2    van Hage-Hamsten, M.3    Achour, A.4
  • 7
    • 0026556059 scopus 로고
    • Pheromone binding proteins of the mouse, Mus musculus
    • Bacchini A., Gaetani E., Cavaggioni A. Pheromone binding proteins of the mouse, Mus musculus. Experientia 1992, 48:419-421.
    • (1992) Experientia , vol.48 , pp. 419-421
    • Bacchini, A.1    Gaetani, E.2    Cavaggioni, A.3
  • 8
    • 0039171139 scopus 로고    scopus 로고
    • Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes
    • Lascombe M.B., Gregoire C., Poncet P., Tavares G.A., Rosinski-Chupin I., Rabillon J. Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes. J. Biol. Chem. 2000, 275:21572-21577.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21572-21577
    • Lascombe, M.B.1    Gregoire, C.2    Poncet, P.3    Tavares, G.A.4    Rosinski-Chupin, I.5    Rabillon, J.6
  • 9
    • 0030777937 scopus 로고    scopus 로고
    • The major dog allergens, Can f 1 and Can f 2, are salivary lipocalin proteins: cloning and immunological characterization of the recombinant forms
    • Konieczny A., Morgenstern J.P., Bizinkauskas C.B., Lilley C.H., Brauer A.W., Bond J.F., et al. The major dog allergens, Can f 1 and Can f 2, are salivary lipocalin proteins: cloning and immunological characterization of the recombinant forms. Immunology 1997, 92:577-586.
    • (1997) Immunology , vol.92 , pp. 577-586
    • Konieczny, A.1    Morgenstern, J.P.2    Bizinkauskas, C.B.3    Lilley, C.H.4    Brauer, A.W.5    Bond, J.F.6
  • 11
    • 0025771560 scopus 로고
    • Affinity purification of a major and a minor allergen from dog extract: serologic activity of affinity-purified Can f I and of Can f I-depleted extract
    • de Groot H., Goei K.G.H., van Swieten P., Aalberse R.C. Affinity purification of a major and a minor allergen from dog extract: serologic activity of affinity-purified Can f I and of Can f I-depleted extract. J. Allergy Clin. Immunol. 1991, 87:1056-1065.
    • (1991) J. Allergy Clin. Immunol. , vol.87 , pp. 1056-1065
    • de Groot, H.1    Goei, K.G.H.2    van Swieten, P.3    Aalberse, R.C.4
  • 12
    • 0025794175 scopus 로고
    • Purification and characterization of the major dog allergen, Can f I
    • Schou C., Svendsen U.G., Lowenstein H. Purification and characterization of the major dog allergen, Can f I. Clin. Exp. Allergy 1991, 21:321-328.
    • (1991) Clin. Exp. Allergy , vol.21 , pp. 321-328
    • Schou, C.1    Svendsen, U.G.2    Lowenstein, H.3
  • 14
    • 0033406733 scopus 로고    scopus 로고
    • Important animal allergens are lipocalin proteins: why are they allergenic?
    • Virtanen T., Zeiler T., Mantyjarvi R. Important animal allergens are lipocalin proteins: why are they allergenic?. Int. Arch. Allergy Immunol. 1999, 120:247-258.
    • (1999) Int. Arch. Allergy Immunol. , vol.120 , pp. 247-258
    • Virtanen, T.1    Zeiler, T.2    Mantyjarvi, R.3
  • 15
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: structure and function
    • Flower D.R. The lipocalin protein family: structure and function. Biochem. J. 1996, 318:1-14.
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 16
    • 0034684227 scopus 로고    scopus 로고
    • Experimentally determined lipocalin structures
    • Flower D.R. Experimentally determined lipocalin structures. Biochim. Biophys. Acta 2000, 1482:46-56.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 46-56
    • Flower, D.R.1
  • 17
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: structural and sequence overview
    • Flower D.R., North A.C., Sansom C.E. The lipocalin protein family: structural and sequence overview. Biochim. Biophys. Acta 2000, 1482:9-24.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 18
    • 0029294696 scopus 로고
    • Multiple molecular recognition properties of the lipocalin protein family
    • Flower D.R. Multiple molecular recognition properties of the lipocalin protein family. J. Mol. Recognit. 1995, 8:185-195.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 185-195
    • Flower, D.R.1
  • 19
    • 0027302351 scopus 로고
    • Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein
    • Zanotti G., Berni R., Monaco H.L. Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein. J. Biol. Chem. 1993, 268:10728-10738.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10728-10738
    • Zanotti, G.1    Berni, R.2    Monaco, H.L.3
  • 20
    • 0027176956 scopus 로고
    • Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 Å resolution
    • Zanotti G., Ottonello S., Berni R., Monaco H.L. Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 Å resolution. J. Mol. Biol. 1993, 230:613-624.
    • (1993) J. Mol. Biol. , vol.230 , pp. 613-624
    • Zanotti, G.1    Ottonello, S.2    Berni, R.3    Monaco, H.L.4
  • 21
    • 0026475945 scopus 로고
    • Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
    • Bocskei Z., Groom C.R., Flower D.R., Wright C.E., Phillips S.E., Cavaggioni A., et al. Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography. Nature 1992, 360:186-188.
    • (1992) Nature , vol.360 , pp. 186-188
    • Bocskei, Z.1    Groom, C.R.2    Flower, D.R.3    Wright, C.E.4    Phillips, S.E.5    Cavaggioni, A.6
  • 26
    • 0025286532 scopus 로고
    • Crystallographic refinement of human serum retinol binding protein at 2 Å resolution
    • Cowan S.W., Newcomer M.E., Jones T.A. Crystallographic refinement of human serum retinol binding protein at 2 Å resolution. Proteins: Struct. Funct. Bioinformatics 1990, 8:44-61.
    • (1990) Proteins: Struct. Funct. Bioinformatics , vol.8 , pp. 44-61
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 28
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E.E. Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 1987, 197:695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 29
    • 0022931198 scopus 로고
    • The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein
    • Papiz M.Z., Sawyer L., Eliopoulos E.E., North A.C., Findlay J.B., Sivaprasadarao R., et al. The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986, 324:383-385.
    • (1986) Nature , vol.324 , pp. 383-385
    • Papiz, M.Z.1    Sawyer, L.2    Eliopoulos, E.E.3    North, A.C.4    Findlay, J.B.5    Sivaprasadarao, R.6
  • 31
    • 35649024789 scopus 로고    scopus 로고
    • Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D
    • Eichinger A., Nasreen A., Kim H.J., Skerra A. Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D. J. Biol. Chem. 2007, 282:31068-31075.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31068-31075
    • Eichinger, A.1    Nasreen, A.2    Kim, H.J.3    Skerra, A.4
  • 32
    • 12844277300 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands
    • Breustedt D.A., Korndorfer I.P., Redl B., Skerra A. The 1.8 Å crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands. J. Biol. Chem. 2005, 280:484-493.
    • (2005) J. Biol. Chem. , vol.280 , pp. 484-493
    • Breustedt, D.A.1    Korndorfer, I.P.2    Redl, B.3    Skerra, A.4
  • 33
    • 70349596306 scopus 로고    scopus 로고
    • A new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavity
    • Breustedt D.A., Chatwell L., Skerra A. A new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavity. Acta Crystallogr. D 2009, 65:1118-1125.
    • (2009) Acta Crystallogr. D , vol.65 , pp. 1118-1125
    • Breustedt, D.A.1    Chatwell, L.2    Skerra, A.3
  • 35
    • 11844301598 scopus 로고    scopus 로고
    • Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration
    • Holmes M.A., Paulsene W., Jide X., Ratledge C., Strong R.K. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure 2005, 13:29-41.
    • (2005) Structure , vol.13 , pp. 29-41
    • Holmes, M.A.1    Paulsene, W.2    Jide, X.3    Ratledge, C.4    Strong, R.K.5
  • 36
    • 0028149038 scopus 로고
    • Structural analysis and classification of lipocalins and related proteins using a profile-search method
    • Sansom C.E., North A.C., Sawyer L. Structural analysis and classification of lipocalins and related proteins using a profile-search method. Biochim. Biophys. Acta 1994, 1208:247-255.
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 247-255
    • Sansom, C.E.1    North, A.C.2    Sawyer, L.3
  • 37
    • 0035910275 scopus 로고    scopus 로고
    • Crystal structure of aphrodisin, a sex pheromone from female hamster
    • Vincent F., Lobel D., Brown K., Spinelli S., Grote P., Breer H., et al. Crystal structure of aphrodisin, a sex pheromone from female hamster. J. Mol. Biol. 2001, 305:459-469.
    • (2001) J. Mol. Biol. , vol.305 , pp. 459-469
    • Vincent, F.1    Lobel, D.2    Brown, K.3    Spinelli, S.4    Grote, P.5    Breer, H.6
  • 38
    • 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., Cambillau C. Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/androstenone docking simulations. Eur. J. Biochem. 2002, 269:2449-2456.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2449-2456
    • Spinelli, S.1    Vincent, F.2    Pelosi, P.3    Tegoni, M.4    Cambillau, C.5
  • 39
    • 0034775160 scopus 로고    scopus 로고
    • Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily
    • Greene L.H., Chrysina E.D., Irons L.I., Papageorgiou A.C., Acharya K.R., Brew K. Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. Protein Sci. 2001, 10:2301-2316.
    • (2001) Protein Sci. , vol.10 , pp. 2301-2316
    • Greene, L.H.1    Chrysina, E.D.2    Irons, L.I.3    Papageorgiou, A.C.4    Acharya, K.R.5    Brew, K.6
  • 40
    • 67449094947 scopus 로고    scopus 로고
    • Production, crystallization and preliminary X-ray diffraction analysis of the allergen Can f 2 from Canis familiaris
    • Madhurantakam C., Nilsson O.B., Jonsson K., Grönlund H., Achour A. Production, crystallization and preliminary X-ray diffraction analysis of the allergen Can f 2 from Canis familiaris. Acta Crystallogr. F 2009, 65:467-471.
    • (2009) Acta Crystallogr. F , vol.65 , pp. 467-471
    • Madhurantakam, C.1    Nilsson, O.B.2    Jonsson, K.3    Grönlund, H.4    Achour, A.5
  • 43
    • 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., Tegoni M. The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry 1998, 37:7913-7918.
    • (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
  • 45
    • 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., Cambillau C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nat. Struct. Biol. 1996, 3:863-867.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 863-867
    • Tegoni, M.1    Ramoni, R.2    Bignetti, E.3    Spinelli, S.4    Cambillau, C.5
  • 46
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 1995, 20:478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 47
    • 34848895087 scopus 로고    scopus 로고
    • Crystal structure of complement protein C8γ in complex with a peptide containing the C8γ binding site on C8α: implications for C8γ ligand binding
    • Lovelace L.L., Chiswell B., Slade D.J., Sodetz J.M., Lebioda L. Crystal structure of complement protein C8γ in complex with a peptide containing the C8γ binding site on C8α: implications for C8γ ligand binding. Mol. Immunol. 2008, 45:750-756.
    • (2008) Mol. Immunol. , vol.45 , pp. 750-756
    • Lovelace, L.L.1    Chiswell, B.2    Slade, D.J.3    Sodetz, J.M.4    Lebioda, L.5
  • 48
    • 0033515058 scopus 로고    scopus 로고
    • The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP
    • Naylor H.M., Newcomer M.E. The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP. Biochemistry 1999, 38:2647-2653.
    • (1999) Biochemistry , vol.38 , pp. 2647-2653
    • Naylor, H.M.1    Newcomer, M.E.2
  • 49
    • 0028086287 scopus 로고
    • A major continuous allergenic epitope of bovine beta-lactoglobulin recognized by human IgE binding
    • Ball G., Shelton M.J., Walsh B.J., Hill D.J., Hosking C.S., Howden M.E. A major continuous allergenic epitope of bovine beta-lactoglobulin recognized by human IgE binding. Clin. Exp. Allergy 1994, 24:758-764.
    • (1994) Clin. Exp. Allergy , vol.24 , pp. 758-764
    • Ball, G.1    Shelton, M.J.2    Walsh, B.J.3    Hill, D.J.4    Hosking, C.S.5    Howden, M.E.6
  • 50
    • 33751099863 scopus 로고    scopus 로고
    • Prediction of residues in discontinuous B-cell epitopes using protein 3D structures
    • Haste A.P., Nielsen M., Lund O. Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Protein Sci. 2006, 15:2558-2567.
    • (2006) Protein Sci. , vol.15 , pp. 2558-2567
    • Haste, A.P.1    Nielsen, M.2    Lund, O.3
  • 52
    • 1642315560 scopus 로고    scopus 로고
    • Polyreactivity of antibody molecules
    • Notkins A.L. Polyreactivity of antibody molecules. Trends Immunol. 2004, 25:174-179.
    • (2004) Trends Immunol. , vol.25 , pp. 174-179
    • Notkins, A.L.1
  • 53
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James L.C., Roversi P., Tawfik D.S. Antibody multispecificity mediated by conformational diversity. Science 2003, 299:1362-1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 54
    • 62849095162 scopus 로고    scopus 로고
    • Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site
    • Bostrom J., Yu S.F., Kan D., Appleton B.A., Lee C.V., Billeci K., et al. Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site. Science 2009, 323:1610-1614.
    • (2009) Science , vol.323 , pp. 1610-1614
    • Bostrom, J.1    Yu, S.F.2    Kan, D.3    Appleton, B.A.4    Lee, C.V.5    Billeci, K.6
  • 55
    • 62849092568 scopus 로고    scopus 로고
    • Immunology. Two-in-one designer antibodies
    • Parren P.W., Burton D.R. Immunology. Two-in-one designer antibodies. Science 2009, 323:1567-1568.
    • (2009) Science , vol.323 , pp. 1567-1568
    • Parren, P.W.1    Burton, D.R.2
  • 56
    • 33644877464 scopus 로고    scopus 로고
    • Protein microarrays for the diagnosis of allergic diseases: state-of-the-art and future development
    • Harwanegg C., Hiller R. Protein microarrays for the diagnosis of allergic diseases: state-of-the-art and future development. Clin. Chem. Lab Med. 2005, 43:1321-1326.
    • (2005) Clin. Chem. Lab Med. , vol.43 , pp. 1321-1326
    • Harwanegg, C.1    Hiller, R.2
  • 58
    • 0141960041 scopus 로고    scopus 로고
    • Formation of disulfide bonds and homodimers of the major cat allergen Fel d 1 equivalent to the natural allergen by expression in Escherichia coli
    • Grönlund H., Bergman T., Sandstrom K., Alvelius G., Reininger R., Verdino P., et al. Formation of disulfide bonds and homodimers of the major cat allergen Fel d 1 equivalent to the natural allergen by expression in Escherichia coli. J. Biol. Chem. 2003, 278:40144-40151.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40144-40151
    • Grönlund, H.1    Bergman, T.2    Sandstrom, K.3    Alvelius, G.4    Reininger, R.5    Verdino, P.6
  • 59
    • 0028017378 scopus 로고
    • Allergenic characterization of Acarus siro and Tyrophagus putrescentiae and their crossreactivity with Lepidoglyphus destructor and Dermatophagoides pteronyssinus
    • Johansson E., Johansson S.G., van Hage-Hamsten M. Allergenic characterization of Acarus siro and Tyrophagus putrescentiae and their crossreactivity with Lepidoglyphus destructor and Dermatophagoides pteronyssinus. Clin. Exp. Allergy 1994, 24:743-751.
    • (1994) Clin. Exp. Allergy , vol.24 , pp. 743-751
    • Johansson, E.1    Johansson, S.G.2    van Hage-Hamsten, M.3
  • 61
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989, 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 62
    • 0037541076 scopus 로고    scopus 로고
    • Cloning and characterisation of two IgE-binding proteins, homologous to tropomyosin and alpha-tubulin, from the mite Lepidoglyphus destructor
    • Saarne T., Kaiser L., Rasool O., Huecas S., van Hage-Hamsten M., Gafvelin G. Cloning and characterisation of two IgE-binding proteins, homologous to tropomyosin and alpha-tubulin, from the mite Lepidoglyphus destructor. Int. Arch. Allergy Immunol. 2003, 130:258-265.
    • (2003) Int. Arch. Allergy Immunol. , vol.130 , pp. 258-265
    • Saarne, T.1    Kaiser, L.2    Rasool, O.3    Huecas, S.4    van Hage-Hamsten, M.5    Gafvelin, G.6
  • 63
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. D 2006, 62:48-57.
    • (2006) Acta Crystallogr. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 64
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Acta Crystallogr. D 1994, 50:760-763. The CCP4 suite: programs for protein crystallography.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 66
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin V.S., Wilson K.S. Automated refinement of protein models. Acta Crystallogr. D 1993, 49:129-147.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 67
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 68
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn M.D., Murshudov G.N., Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 2003, 374:300-321.
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 69
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: a sketchpad for protein structure topology cartoons
    • Bond C.S. TopDraw: a sketchpad for protein structure topology cartoons. Bioinformatics 2003, 19:311-312.
    • (2003) Bioinformatics , vol.19 , pp. 311-312
    • Bond, C.S.1
  • 70
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 71
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins
    • Binkowski T.A., Naghibzadeh S., Liang J. CASTp: computed atlas of surface topography of proteins. Nucleic Acids Res. 2003, 31:3352-3355.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 72
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999, 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 73
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.