Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity

Birthe R Johannessen; Lars Skov; Jette S Kastrup; Ole Kristensen; Caroline Bolwig; Jørgen Larsen; Michael Spangfort; Kaare Lund; Michael Gajhede

doi:10.1016/j.febslet.2004.11.115

Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity

Birthe R Johannessen, Lars Skov, Jette S Kastrup, Ole Kristensen, Caroline Bolwig, Jørgen Larsen, Michael Spangfort, Kaare Lund, Michael Gajhede

41 Citationer (Scopus)

Abstract

The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.

Originalsprog	Engelsk
Tidsskrift	F E B S Letters
Vol/bind	579
Udgave nummer	5
Sider (fra-til)	1208-12
Antal sider	5
ISSN	0014-5793
DOI	https://doi.org/10.1016/j.febslet.2004.11.115
Status	Udgivet - 2005

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10.1016/j.febslet.2004.11.115

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title = "Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity",

abstract = "The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.",

keywords = "Allergens, Animals, Antigens, Dermatophagoides, Arthropod Proteins, Cross Reactions, Crystallography, X-Ray, Epitopes, Hydrophobic and Hydrophilic Interactions, Immunoglobulin E, Lipid Metabolism, Models, Molecular, Protein Structure, Tertiary, Pyroglyphidae",

author = "Johannessen, {Birthe R} and Lars Skov and Kastrup, {Jette S} and Ole Kristensen and Caroline Bolwig and J{\o}rgen Larsen and Michael Spangfort and Kaare Lund and Michael Gajhede",

year = "2005",

doi = "10.1016/j.febslet.2004.11.115",

language = "English",

volume = "579",

pages = "1208--12",

journal = "F E B S Letters",

issn = "0014-5793",

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TY - JOUR

T1 - Structure of the house dust mite allergen Der f 2

T2 - implications for function and molecular basis of IgE cross-reactivity

AU - Johannessen, Birthe R

AU - Skov, Lars

AU - Kastrup, Jette S

AU - Kristensen, Ole

AU - Bolwig, Caroline

AU - Larsen, Jørgen

AU - Spangfort, Michael

AU - Lund, Kaare

AU - Gajhede, Michael

PY - 2005

Y1 - 2005

N2 - The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.

AB - The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.

KW - Allergens

KW - Animals

KW - Antigens, Dermatophagoides

KW - Arthropod Proteins

KW - Cross Reactions

KW - Crystallography, X-Ray

KW - Epitopes

KW - Hydrophobic and Hydrophilic Interactions

KW - Immunoglobulin E

KW - Lipid Metabolism

KW - Models, Molecular

KW - Protein Structure, Tertiary

KW - Pyroglyphidae

U2 - 10.1016/j.febslet.2004.11.115

DO - 10.1016/j.febslet.2004.11.115

M3 - Journal article

C2 - 15710415

SN - 0014-5793

VL - 579

SP - 1208

EP - 1212

JO - F E B S Letters

JF - F E B S Letters

IS - 5

ER -

Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity

Abstract

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