Crystal structure of a sweet tasting protein thaumatin I, at 1·65 Å resolution

Ogata, Craig M.; Gordon, P. F.; Vos, Abraham M. de; Kim, Sung‐Hou

doi:10.1016/0022-2836(92)90873-i

Cited by 112 publications

(56 citation statements)

References 51 publications

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“…The predicted mass of the mature protein is 21,286.45 D, whereas that obtained by MS is 21,272.90 ± 1.88 D. The discrepancy of 16 D is accounted for by the formation of eight disulfide bonds, as seen in crystallized thaumatin (Ogata et al, 1992). Thus, we conclude not only that the cDNA sequence (Fig.…”

Section: Polypeptide Pattern Of Developing Grape Berriesmentioning

confidence: 70%

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

1997

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Section: Polypeptide Pattern Of Developing Grape Berriesmentioning

confidence: 70%

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

1997

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“…This highly stabilized structure allows PR-5 proteins to be very resistant to protease degradation (148). The X-ray structures have been determined for two PR-5 proteins and thaumatin (82,134).…”

Section: Fungal Cell Wall Structurementioning

confidence: 99%

Antifungal Proteins

Selitrennikoff

2001

Appl Environ Microbiol

526

362

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“…No glycosylation has been reported from any TLP so far. The structure of thaumatin I has been determined by X-ray crystallography [52]. The locations of the cysteines are highly conserved between other high molecular weight members of the PR-5 family.…”

Section: Pr-5 – Thaumatin-like Proteins (Tlps)mentioning

confidence: 99%

Plant Allergens and Pathogenesis-Related Proteins

Hoffmann‐Sommergruber

2000

Int Arch Allergy Immunol

171

114

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In the recent past a great number of proteins causing type 1 allergic reactions in humans have been isolated and characterised. The main sources containing allergens are plants, mites, fungal spores and insects. Plant-derived allergens may either be taken in from the upper respiratory tract or they are present in a vast range of plant food causing food allergic reactions. Compared to the enormous amount of different plant proteins only a small number out of them are identified as a an allergen at present. Looking at the allergen encoding sequences, relationships by sequence similarity can be found quite frequently to a restricted number of plant protein families. Predominantly, these protein families are seed storage proteins, structural proteins and proteins involved in the defence-related system – pathogenesis-related proteins. In the following, a short overview of a number of pathogenesis-related protein families is presented in relation to the already known homologous plant allergens.

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Crystal structure of a sweet tasting protein thaumatin I, at 1·65 Å resolution

Cited by 112 publications

References 51 publications

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

Identification and Characterization of a Fruit-Specific, Thaumatin-Like Protein That Accumulates at Very High Levels in Conjunction with the Onset of Sugar Accumulation and Berry Softening in Grapes

Antifungal Proteins

Plant Allergens and Pathogenesis-Related Proteins

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