Related ArticlesNMR resonance assignments of the major apple allergen Mal d 1.
Biomol NMR Assign. 2016 May 11;
Authors: Ahammer L, Grutsch S, Tollinger M
Abstract
The major apple allergen Mal d 1 is the predominant cause of apple (Malus domestica) allergies in large parts of Europe and Northern America. Allergic reactions against this 17.5*kDa protein are the consequence of initial sensitization to the structurally homologous major allergen from birch pollen, Bet v 1. Consumption of apples can subsequently provoke immunologic cross-reactivity of Bet v 1-specific antibodies with Mal d 1 and trigger severe oral allergic syndroms, affecting more than 70*% of all individuals that are sensitized to birch pollen. While the accumulated immunological data suggest that Mal d 1 has a three-dimensional fold that is similar to Bet v 1, experimental structural data for this protein are not available to date. In a first step towards structural characterization of Mal d 1, backbone and side chain (1)H, (13)C and (15)N chemical shifts of the isoform Mal d 1.0101 were assigned. The NMR-chemical shift data show that this protein is composed of seven ?-strands and three ?-helices, which is in accordance with the reported secondary structure of the major birch pollen allergen, indicating that Mal d 1 and Bet v 1 indeed have similar three-dimensional folds. The next stage in the characterization of Mal d 1 will be to utilize these resonance assignments in solving the solution structure of this protein.
PMID: 27165578 [PubMed - as supplied by publisher]
[NMR paper] NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins.
NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins.
Related Articles NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins.
Structure. 2015 May 12;
Authors: Zook J, Mo G, Sisco NJ, Craciunescu FM, Hansen DT, Baravati B, Cherry BR, Sykes K, Wachter R, Van Horn WD, Fromme P
Abstract
Tularemia is a potentially fatal bacterial infection caused by Francisella tularensis, and is endemic to North America and...
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05-26-2015 08:09 PM
NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins
NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins
Publication date: Available online 21 May 2015
Source:Structure</br>
Author(s): James Zook , Gina Mo , Nicholas*J. Sisco , Felicia*M. Craciunescu , Debra*T. Hansen , Bobby Baravati , Brian*R. Cherry , Kathryn Sykes , Rebekka Wachter , Wade*D. Van*Horn , Petra Fromme</br>
Tularemia is a potentially fatal bacterial infection caused by Francisella tularensis, and is endemic to North America and many parts of northern Europe and Asia. The outer...
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05-21-2015 04:28 PM
[NMRpipe Yahoo group] Re: nmrPipe, XQuartz and Apple's Software Update
Re: nmrPipe, XQuartz and Apple's Software Update
Hello everybody, I have a MacBookPro running 10.6.6. I have installed the latest version of nmrPipe and I got into the bus error mentioned in this thread.
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[NMR paper] NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitope
NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
Related Articles NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
J Biochem. 2005 Mar;137(3):255-63
Authors: Ichikawa S, Takai T, Inoue T, Yuuki T, Okumura Y, Ogura K, Inagaki F, Hatanaka H
Group 2 major mite allergens Der f 2 and Der p 2 are classified into...
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11-24-2010 11:14 PM
[NMR paper] Recombinant expression of Ole e 6, a Cys-enriched pollen allergen, in Pichia pastoris
Recombinant expression of Ole e 6, a Cys-enriched pollen allergen, in Pichia pastoris yeast: detection of partial oxidation of methionine by NMR.
Related Articles Recombinant expression of Ole e 6, a Cys-enriched pollen allergen, in Pichia pastoris yeast: detection of partial oxidation of methionine by NMR.
Protein Expr Purif. 2004 Oct;37(2):336-43
Authors: Barral P, Tejera ML, Treviño MA, Batanero E, Villalba M, Bruix M, Rodríguez R
Olive pollen is one of the main causes of allergy in Mediterranean countries. Ole e 6, an olive pollen...
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11-24-2010 10:01 PM
[NMR paper] NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
Related Articles NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
J Biol Chem. 2004 Sep 10;279(37):39035-41
Authors: Treviño MA, García-Mayoral MF, Barral P, Villalba M, Santoro J, Rico M, Rodríguez R, Bruix M
Ole e 6 is a pollen protein from the olive tree (Olea europaea) that exhibits allergenic activity with a high prevalence among olive-allergic individuals. The three-dimensional structure of Ole e 6 has been determined in solution by NMR...
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[NMRpipe Yahoo group] Re: nmrPipe, XQuartz and Apple's Software Update
Re: nmrPipe, XQuartz and Apple's Software Update
Yes, I think that's what I have too, Ryan. I get the bus error with 10.6.4 and XQuartz 2.5.3, i.e. if the XQuartz install was the last thing I did. Haven't yet
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NMR resonance assignments of the major apple allergen Mal d 1.
Linear Mode
