Linked Life Data

20553495

Source:http://linkedlifedata.com/resource/pubmed/id/20553495

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-6-17
pubmed:abstractText
Polcalcins such as Bet v 4 and Phl p 7 are pollen allergens that are constructed from EF-hand motifs, which are very common and well characterized helix-loop-helix motifs with calcium-binding functions, as elementary building blocks. Being members of an exceptionally well-characterized protein superfamily, these allergens highlight the fundamental challenge in explaining what features distinguish allergens from nonallergenic proteins. We found that Bet v 4 and Phl p 7 undergo oligomerization transitions with characteristics that are markedly different from those typically found in proteins: transitions from monomers to dimers and to distinct higher oligomers can be induced by increasing temperature; similarly, low concentrations of destabilizing agents, e.g. SDS, induce oligomerization transitions of Bet v 4. The changes in the quaternary structure, termed molecular metamorphosis, are induced and controlled by a combination of EF-hand rearrangements and domain swapping rather than by the classical law of mass action. Using an EF-hand-pairing model, we provide a two-step model that consistently explains and substantiates the observed metamorphosis. Moreover, the unusual oligomerization behavior suggests a straightforward explanation of how allergens can accomplish the crosslinking of IgE on mast cells, a hallmark of allergens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1742-4658
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2598-610
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Molecular metamorphosis in polcalcin allergens by EF-hand rearrangements and domain swapping.
pubmed:affiliation
Division of Structural Biology, Department of Molecular Biology, University of Salzburg, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't