English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons92829

Eschenburg,  Susanne
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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 Crystallographica Section D-Biological Crystallography, 58(7), 1175-1181. doi:10.1107/S0907444902007254.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-7829-B
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'.