This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2a0a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a0a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2a0a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2a0a| PDB=2a0a | SCENE= }}
{{STRUCTURE_2a0a| PDB=2a0a | SCENE= }}
-
'''Solution Structure of Der f 13, Group 13 Allergen from House Dust Mites'''
+
===Solution Structure of Der f 13, Group 13 Allergen from House Dust Mites===
-
==Overview==
+
<!--
-
IgE-mediated allergic response involves cross-linking of IgE bound on mast cells by specific surface epitopes of allergens. Structural studies on IgE epitopes of allergens are essential in understanding the characteristics of an allergen and for development of specific allergen immunotherapy. We have determined the structure of a group 13 dust mite allergen from Dermatophagoides farinae, Der f 13, using nuclear magnetic resonance. Sequence comparison of Der f 13 with homologous human fatty acid-binding proteins revealed unique surface charged residues on Der f 13 that may be involved in IgE binding and allergenicity. Site-directed mutagenesis and IgE binding assays have confirmed four surface charged residues on opposite sides of the protein that are involved in IgE binding. A triple mutant of Der f 13 (E41A_K63A_K91A) has been generated and found to have significantly reduced IgE binding and histamine release in skin prick tests on patients allergenic to group 13 dust mite allergens. The triple mutant is also able to induce PBMC proliferation in allergic patients with indices similar to those of wild-type Der f 13 and shift the secretion of cytokines from a Th2 to a Th1 pattern. Mouse IgG serum raised using the triple mutant is capable to block the binding of IgE from allergic patients to wild-type Der f 13, indicating potential for the triple mutant as a hypoallergen for specific immunotherapy. Findings in this study imply the importance of surface charged residues on IgE binding and allergenicity of an allergen, as was also demonstrated in other major allergens studied.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16585580}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16585580 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16585580}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0A OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0A OCA].
==Reference==
==Reference==
Line 24: Line 28:
[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Helix]]
[[Category: Helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:26:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:10:59 2008''

Revision as of 20:11, 27 July 2008

Image:2a0a.png

Template:STRUCTURE 2a0a

Solution Structure of Der f 13, Group 13 Allergen from House Dust Mites

Template:ABSTRACT PUBMED 16585580

About this Structure

Full experimental information is available from OCA.

Reference

Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen., Chan SL, Ong ST, Ong SY, Chew FT, Mok YK, J Immunol. 2006 Apr 15;176(8):4852-60. PMID:16585580

Page seeded by OCA on Sun Jul 27 23:10:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a0a"
Personal tools