1bmw
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1bmw.gif|left|200px]] | [[Image:1bmw.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1bmw", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1bmw| PDB=1bmw | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''A FIBRONECTIN TYPE III FOLD IN PLANT ALLERGENS: THE SOLUTION STRUCTURE OF PHL PII FROM TIMOTHY GRASS POLLEN, NMR, 38 STRUCTURES''' | '''A FIBRONECTIN TYPE III FOLD IN PLANT ALLERGENS: THE SOLUTION STRUCTURE OF PHL PII FROM TIMOTHY GRASS POLLEN, NMR, 38 STRUCTURES''' | ||
| Line 34: | Line 31: | ||
[[Category: Valenta, R.]] | [[Category: Valenta, R.]] | ||
[[Category: Vrtala, S.]] | [[Category: Vrtala, S.]] | ||
| - | [[Category: | + | [[Category: Allergen]] |
| - | [[Category: | + | [[Category: Allergy]] |
| - | [[Category: | + | [[Category: Immunoglobulin]] |
| - | [[Category: | + | [[Category: Immunology]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:42:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:42, 2 May 2008
A FIBRONECTIN TYPE III FOLD IN PLANT ALLERGENS: THE SOLUTION STRUCTURE OF PHL PII FROM TIMOTHY GRASS POLLEN, NMR, 38 STRUCTURES
Overview
BACKGROUND: Grass pollen allergens are the most important and widespread elicitors of pollen allergy. One of the major plant allergens which millions of people worldwide are sensitized to is Phl p 2, a small protein from timothy grass pollen. Phl p 2 is representative of the large family of cross-reacting plant allergens classified as group 2/3. Recombinant Phl p 2 has been demonstrated by immunological cross-reactivity studies to be immunologically equivalent to the natural protein. RESULTS: We have solved the solution structure of recombinant Phl p 2 by means of nuclear magnetic resonance techniques. The three-dimensional structure of Phl p 2 consists of an all-beta fold with nine antiparallel beta strands that form a beta sandwich. The topology is that of an immunoglobulin-like fold with the addition of a C-terminal strand, as found in the C2 domain superfamily. Lack of functional and sequence similarity with these two families, however, suggests an independent evolution of Phl p 2 and other homologous plant allergens. CONCLUSIONS: Because of the high homology with other plant allergens of groups 1 and 2/3, the structure of Phl p 2 can be used to rationalize some of the immunological properties of the whole family. On the basis of the structure, we suggest possible sites of interaction with IgE antibodies. Knowledge of the Phl p 2 structure may assist the rational structure-based design of synthetic vaccines against grass pollen allergy.
About this Structure
1BMW is a Single protein structure of sequence from Phleum pratense. Full crystallographic information is available from OCA.
Reference
An immunoglobulin-like fold in a major plant allergen: the solution structure of Phl p 2 from timothy grass pollen., De Marino S, Morelli MA, Fraternali F, Tamborini E, Musco G, Vrtala S, Dolecek C, Arosio P, Valenta R, Pastore A, Structure. 1999 Aug 15;7(8):943-52. PMID:10467147 Page seeded by OCA on Fri May 2 11:42:53 2008
