1puo: Difference between revisions
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==Crystal structure of Fel d 1- the major cat allergen== | ==Crystal structure of Fel d 1- the major cat allergen== | ||
<StructureSection load='1puo' size='340' side='right' caption='[[1puo]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1puo' size='340' side='right'caption='[[1puo]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1puo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cat Cat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PUO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1puo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cat Cat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PUO FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cat]] | [[Category: Cat]] | ||
[[Category: Large Structures]] | |||
[[Category: Achour, A]] | [[Category: Achour, A]] | ||
[[Category: Gronlund, H]] | [[Category: Gronlund, H]] | ||
Revision as of 09:12, 3 July 2019
Crystal structure of Fel d 1- the major cat allergenCrystal structure of Fel d 1- the major cat allergen
Structural highlights
Publication Abstract from PubMedThe domestic cat (Felis domesticus) is one of the most important causes of allergic asthma worldwide. The dominating cat allergen, Fel d 1, is composed of two heterodimers. Recently, it has been shown that recombinant Fel d 1, consisting of chain 2 and chain 1 fused together without additional linker, has immunological properties indistinguishable from the natural heterodimeric protein. Herein, we report the crystal structure of recombinant monomeric Fel d 1 at 1.85-A resolution, determined by multi-wavelength anomalous diffraction using selenomethionine substituted protein. Fel d 1 is an all-helical protein and consists of eight helices. The two halves of the recombinant Fel d 1 molecule, corresponding to the wild-type Fel d 1 chains, are very similar in three-dimensional structure, despite the lack of significant sequence identity. The structure of the Fel d 1 presents a striking similarity to that of uteroglobin, a steroid-inducible cytokine-like molecule with anti-inflammatory and immunomodulatory properties. An internal, asymmetric cavity is formed in the Fel d 1 that could bind an endogenous ligand. The distribution of residues lining this cavity suggests that such a ligand must be amphipathic. The structure of Fel d 1 displays the localization of three previously defined Fel d 1 IgE epitopes on the surface of the protein. The three-dimensional structure provides a framework for rational design of hypoallergenic mutants aimed for treatment of cat allergy. The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family.,Kaiser L, Gronlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G J Biol Chem. 2003 Sep 26;278(39):37730-5. Epub 2003 Jul 8. PMID:12851385[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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