1fm4
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1fm4.gif|left|200px]] | [[Image:1fm4.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1fm4", 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_1fm4| PDB=1fm4 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF THE BIRCH POLLEN ALLERGEN BET V 1L''' | '''CRYSTAL STRUCTURE OF THE BIRCH POLLEN ALLERGEN BET V 1L''' | ||
| Line 34: | Line 31: | ||
[[Category: Scheiner, O.]] | [[Category: Scheiner, O.]] | ||
[[Category: Susani, M.]] | [[Category: Susani, M.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta: 6 anti-parallel beta strands and 3 alpha helices.]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:29:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:29, 2 May 2008
CRYSTAL STRUCTURE OF THE BIRCH POLLEN ALLERGEN BET V 1L
Overview
Bet v 1l is a naturally occurring hypoallergenic isoform of the major birch pollen allergen Bet v 1. The Bet v 1 protein belongs to the ubiquitous family of pathogenesis-related plant proteins (PR-10), which are produced in defense-response to various pathogens. Although the allergenic properties of PR-10 proteins have been extensively studied, their biological function in plants is not known. The crystal structure of Bet v 1l in complex with deoxycholate has been determined to a resolution of 1.9A using the method of molecular replacement. The structure reveals a large hydrophobic Y-shaped cavity that spans the protein and is partly occupied by two deoxycholate molecules which are bound in tandem and only partially exposed to solvent. This finding indicates that the hydrophobic cavity may have a role in facilitating the transfer of apolar ligands. The structural similarity of deoxycholate and brassinosteroids (BRs) ubiquitous plant steroid hormones, prompted the mass spectrometry (MS) study in order to examine whether BRs can bind to Bet v 1l. The MS analysis of a mixture of Bet v 1l and BRs revealed a specific non-covalent interaction of Bet v 1l with brassinolide and 24-epicastasterone. Together, our findings are consistent with a general plant-steroid carrier function for Bet v 1 and related PR-10 proteins. The role of BRs transport in PR-10 proteins may be of crucial importance in the plant defense response to pathological situations as well as in growth and development.
About this Structure
1FM4 is a Single protein structure of sequence from Betula pendula. Full crystallographic information is available from OCA.
Reference
Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier., Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H, J Mol Biol. 2003 Jan 3;325(1):123-33. PMID:12473456 Page seeded by OCA on Fri May 2 16:29:30 2008
