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Structure of the functional domain of the major grass-pollen allergen Phlp 5b.

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Structure of the functional domain of the major grass-pollen allergen Phlp 5b. / Rajashankar, Kanagalaghatta; Bufe, Albrecht; Weber, Wolfgang; Eschenburg, Susanne; Lindner, Buko; Betzel, Christian.

In: ACTA CRYSTALLOGR D, Vol. 58, No. Pt 7, Pt 7, 2002, p. 1175-1181.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Rajashankar, K, Bufe, A, Weber, W, Eschenburg, S, Lindner, B & Betzel, C 2002, 'Structure of the functional domain of the major grass-pollen allergen Phlp 5b.', ACTA CRYSTALLOGR D, vol. 58, no. Pt 7, Pt 7, pp. 1175-1181. <http://www.ncbi.nlm.nih.gov/pubmed/12077438?dopt=Citation>

APA

Rajashankar, K., Bufe, A., Weber, W., Eschenburg, S., Lindner, B., & Betzel, C. (2002). Structure of the functional domain of the major grass-pollen allergen Phlp 5b. ACTA CRYSTALLOGR D, 58(Pt 7), 1175-1181. [Pt 7]. http://www.ncbi.nlm.nih.gov/pubmed/12077438?dopt=Citation

Vancouver

Rajashankar K, Bufe A, Weber W, Eschenburg S, Lindner B, Betzel C. Structure of the functional domain of the major grass-pollen allergen Phlp 5b. ACTA CRYSTALLOGR D. 2002;58(Pt 7):1175-1181. Pt 7.

Bibtex

@article{bfd2ceef91684e6486454422fca45ad0,
title = "Structure of the functional domain of the major grass-pollen allergen Phlp 5b.",
abstract = "The major allergen Phlp 5b from timothy grass pollen induces allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. As an important step towards understanding the interactions between the pollen protein and components of the human immune system, the structure of the C-terminal key domain of Phlp 5b has been determined at 2.0 A resolution and refined to an R value of 19.7%. This is the first known allergen composed entirely of alpha-helices. The protein forms a dimer stabilized by one intermolecular disulfide bridge. Sequence homology suggests that at least all group V and group VI grass-pollen allergens belong to this new class of 'four-helix-bundle allergens'.",
keywords = "Amino Acid Sequence, Molecular Sequence Data, Models, Molecular, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Protein Conformation, Dimerization, Allergens/*chemistry, Crystallography, X-Ray/*methods, Disulfides/chemistry, Poaceae/*chemistry, Pollen/*chemistry, Recombinant Proteins/chemistry, Amino Acid Sequence, Molecular Sequence Data, Models, Molecular, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Protein Conformation, Dimerization, Allergens/*chemistry, Crystallography, X-Ray/*methods, Disulfides/chemistry, Poaceae/*chemistry, Pollen/*chemistry, Recombinant Proteins/chemistry",
author = "Kanagalaghatta Rajashankar and Albrecht Bufe and Wolfgang Weber and Susanne Eschenburg and Buko Lindner and Christian Betzel",
year = "2002",
language = "English",
volume = "58",
pages = "1175--1181",
journal = "ACTA CRYSTALLOGR D",
issn = "2059-7983",
publisher = "John Wiley and Sons Inc.",
number = "Pt 7",

}

RIS

TY - JOUR

T1 - Structure of the functional domain of the major grass-pollen allergen Phlp 5b.

AU - Rajashankar, Kanagalaghatta

AU - Bufe, Albrecht

AU - Weber, Wolfgang

AU - Eschenburg, Susanne

AU - Lindner, Buko

AU - Betzel, Christian

PY - 2002

Y1 - 2002

N2 - The major allergen Phlp 5b from timothy grass pollen induces allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. As an important step towards understanding the interactions between the pollen protein and components of the human immune system, the structure of the C-terminal key domain of Phlp 5b has been determined at 2.0 A resolution and refined to an R value of 19.7%. This is the first known allergen composed entirely of alpha-helices. The protein forms a dimer stabilized by one intermolecular disulfide bridge. Sequence homology suggests that at least all group V and group VI grass-pollen allergens belong to this new class of 'four-helix-bundle allergens'.

AB - The major allergen Phlp 5b from timothy grass pollen induces allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. As an important step towards understanding the interactions between the pollen protein and components of the human immune system, the structure of the C-terminal key domain of Phlp 5b has been determined at 2.0 A resolution and refined to an R value of 19.7%. This is the first known allergen composed entirely of alpha-helices. The protein forms a dimer stabilized by one intermolecular disulfide bridge. Sequence homology suggests that at least all group V and group VI grass-pollen allergens belong to this new class of 'four-helix-bundle allergens'.

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Models, Molecular

KW - Sequence Homology, Amino Acid

KW - Protein Structure, Tertiary

KW - Protein Conformation

KW - Dimerization

KW - Allergens/chemistry

KW - Crystallography, X-Ray/methods

KW - Disulfides/chemistry

KW - Poaceae/chemistry

KW - Pollen/chemistry

KW - Recombinant Proteins/chemistry

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Models, Molecular

KW - Sequence Homology, Amino Acid

KW - Protein Structure, Tertiary

KW - Protein Conformation

KW - Dimerization

KW - Allergens/chemistry

KW - Crystallography, X-Ray/methods

KW - Disulfides/chemistry

KW - Poaceae/chemistry

KW - Pollen/chemistry

KW - Recombinant Proteins/chemistry

M3 - SCORING: Journal article

VL - 58

SP - 1175

EP - 1181

JO - ACTA CRYSTALLOGR D

JF - ACTA CRYSTALLOGR D

SN - 2059-7983

IS - Pt 7

M1 - Pt 7

ER -