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Literature DB >> 17909286

Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3.

Tengchuan Jin¹, Andrew Howard, Yu-Zhu Zhang.

Abstract

The peanut is a significant food source, but is responsible for many cases of anaphylaxis. The peanut 11S legumin-like seed storage protein Ara h 3 is one of the best characterized allergens. In this study, Ara h 3 was extracted from peanut kernels and purified by sequential anion-exchange, hydrophobic interaction and gel-filtration chromatography to very high purity to facilitate crystallization and structural studies. Well diffracting single crystals were obtained by the vapor-diffusion method. A molecular-replacement structural solution has been obtained and refinement of the structure is currently under way.

Entities: Chemical Species

Mesh：

Substances：

Year: 2007 PMID： 17909286 PMCID： PMC2339721 DOI： 10.1107/S1744309107041176

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

14 in total

1. A graph-theory algorithm for rapid protein side-chain prediction.

Authors: Adrian A Canutescu; Andrew A Shelenkov; Roland L Dunbrack
Journal: Protein Sci Date: 2003-09 Impact factor: 6.725

2. Refinement of macromolecular structures by the maximum-likelihood method.

Authors: G N Murshudov; A A Vagin; E J Dodson
Journal: Acta Crystallogr D Biol Crystallogr Date: 1997-05-01

3. Likelihood-enhanced fast rotation functions.

Authors: Laurent C Storoni; Airlie J McCoy; Randy J Read
Journal: Acta Crystallogr D Biol Crystallogr Date: 2004-02-25

4. Likelihood-enhanced fast translation functions.

Authors: Airlie J McCoy; Ralf W Grosse-Kunstleve; Laurent C Storoni; Randy J Read
Journal: Acta Crystallogr D Biol Crystallogr Date: 2005-03-24

5. Organization of the sunflower 11S storage protein gene family.

Authors: R A Vonder Haar; R D Allen; E A Cohen; C L Nessler; T L Thomas
Journal: Gene Date: 1988-12-30 Impact factor: 3.688

Review 6. Current developments in peanut allergy.

Authors: Kricia Palmer; Wesley Burks
Journal: Curr Opin Allergy Clin Immunol Date: 2006-06

7. Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer.

Authors: Motoyasu Adachi; Jiro Kanamori; Taro Masuda; Kazuhiro Yagasaki; Keisuke Kitamura; Bunzo Mikami; Shigeru Utsumi
Journal: Proc Natl Acad Sci U S A Date: 2003-05-27 Impact factor: 11.205

8. A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean.

Authors: M P Scott; R Jung; K Muntz; N C Nielsen
Journal: Proc Natl Acad Sci U S A Date: 1992-01-15 Impact factor: 11.205

Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3.

1. A graph-theory algorithm for rapid protein side-chain prediction.

2. Refinement of macromolecular structures by the maximum-likelihood method.

3. Likelihood-enhanced fast rotation functions.

4. Likelihood-enhanced fast translation functions.

5. Organization of the sunflower 11S storage protein gene family.

Review 6. Current developments in peanut allergy.

7. Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer.

8. A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean.

9. Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization.

10. Crystal structure of soybean proglycinin A1aB1b homotrimer.

1. Purification and crystallization of Cor a 9, a major hazelnut allergen.

Review 2. Structure of allergens and structure based epitope predictions.