PDBsum entry 1ahk

Allergen

PDB id: 1ahk

Contents

Protein chain

129 a.a. *

* Residue conservation analysis

PDB id:

1ahk

Name:

Allergen

Title:

Der f 2, the major mite allergen from dermatophagoides farinae, nmr, minimized average structure

Structure:

Der f 2. Chain: a. Synonym: der f ii. Engineered: yes

Source:

Dermatophagoides farinae. American house dust mite. Organism_taxid: 6954. Cellular_location: extracellular. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

1 models

Authors:

S.Ichikawa,H.Hatanaka,T.Yuuki,N.Iwamoto,K.Ogura,Y.Okumura,F.Inagaki

Key ref:

S.Ichikawa et al. (1998). Solution structure of Der f 2, the major mite allergen for atopic diseases. J Biol Chem, 273, 356-360. PubMed id: 9417088 DOI: 10.1074/jbc.273.1.356

Date:

07-Apr-97 Release date: 08-Apr-98

Protein chain

Q00855  (ALL2_DERFA) -  Mite group 2 allergen Der f 2 from Dermatophagoides farinae

Seq: 146 a.a.

Struc: 129 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1074/jbc.273.1.356

J Biol Chem 273:356-360 (1998)

PubMed id: 9417088

Solution structure of Der f 2, the major mite allergen for atopic diseases.

S.Ichikawa, H.Hatanaka, T.Yuuki, N.Iwamoto, S.Kojima, C.Nishiyama, K.Ogura, Y.Okumura, F.Inagaki.

ABSTRACT

House dust mites cause heavy atopic diseases such as asthma and dermatitis. Among allergens from Dermatophagoides farinae, Der f 2 shows the highest positive rate for atopic patients, but its biological function in mites has been perfectly unknown, as well as the functions of its homologs in human and other animals. We have determined the tertiary structure of Der f 2 by multidimensional nuclear magnetic resonance spectroscopy. Der f 2 was found to be a single-domain protein of immunoglobulin fold, and its structure was the most similar to those of the two regulatory domains of transglutaminase. This fact, binding to the bacterial surface, and other small pieces of information hinted that Der f 2 is related to the innate antibacterial defense system in mites. The immunoglobulin E epitopes are also discussed on the basis of the tertiary structure.

Selected figure(s)

Figure 2.
Fig. 2. Tertiary structure of Der f 2. a, Best fit superpositions of the backbone atoms (N, C^ , C ) of the 10 final structures of Der f 2. Amino acid residue^ numbers are shown every ten residues. b, Ribbon diagrams of the^ mean structure of Der f 2. The start and end residue numbers of^ the -strands are also shown. Both figures were produced by the^ program MOLSCRIPT (44) and shown in stereo. Color changes from red (N terminus) to blue (C terminus).

Figure 5.
Fig. 5. Partial characterization of IgE epitope areas. The molecular surface of Der f 2 was produced by the program GRASP (45) and colored according to the results from the site-directed mutagenesis experiments (42). Red, residues whose substitution decreased^ IgE binding; blue, residues whose substitution did not decrease^ IgE binding; white, residues that were not tested. The top figure^ can be related to Fig. 2 by 105° x rotation, and the bottom can be related to the top by 180° x rotation.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1998, 273, 356-360) copyright 1998.

Figures were selected by an automated process.