2p9w

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[[Image:2p9w.jpg|left|200px]]
[[Image:2p9w.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2p9w |SIZE=350|CAPTION= <scene name='initialview01'>2p9w</scene>, resolution 1.350&Aring;
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The line below this paragraph, containing "STRUCTURE_2p9w", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= Mala s1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=76777 Malassezia sympodialis])
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|DOMAIN=
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{{STRUCTURE_2p9w| PDB=2p9w | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p9w OCA], [http://www.ebi.ac.uk/pdbsum/2p9w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p9w RCSB]</span>
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}}
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'''Crystal Structure of the Major Malassezia sympodialis Allergen Mala s 1'''
'''Crystal Structure of the Major Malassezia sympodialis Allergen Mala s 1'''
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==About this Structure==
==About this Structure==
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2P9W is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Malassezia_sympodialis Malassezia sympodialis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9W OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9W OCA].
==Reference==
==Reference==
Crystal structure of the major Malassezia sympodialis allergen Mala s 1 reveals a beta-propeller fold: a novel fold among allergens., Vilhelmsson M, Zargari A, Crameri R, Rasool O, Achour A, Scheynius A, Hallberg BM, J Mol Biol. 2007 Jun 15;369(4):1079-86. Epub 2007 Apr 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17481656 17481656]
Crystal structure of the major Malassezia sympodialis allergen Mala s 1 reveals a beta-propeller fold: a novel fold among allergens., Vilhelmsson M, Zargari A, Crameri R, Rasool O, Achour A, Scheynius A, Hallberg BM, J Mol Biol. 2007 Jun 15;369(4):1079-86. Epub 2007 Apr 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17481656 17481656]
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[[Category: Malassezia sympodialis]]
 
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[[Category: Protein complex]]
 
[[Category: Achour, A.]]
[[Category: Achour, A.]]
[[Category: Crameri, R.]]
[[Category: Crameri, R.]]
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[[Category: Vilhelmsson, M.]]
[[Category: Vilhelmsson, M.]]
[[Category: Zargari, A.]]
[[Category: Zargari, A.]]
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[[Category: allergen]]
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[[Category: Allergen]]
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[[Category: beta propeller]]
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[[Category: Beta propeller]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:41:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:33:17 2008''
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Revision as of 09:41, 4 May 2008

Template:STRUCTURE 2p9w

Crystal Structure of the Major Malassezia sympodialis Allergen Mala s 1


Overview

Atopic eczema (AE) is a chronic inflammatory disease in which genetic predisposition and environmental factors such as microorganisms contribute to the symptoms. The yeast Malassezia Sympodialis, part of the normal human cutaneous flora, can act as an allergen eliciting specific IgE and T-cell reactivity in patients with AE. The major M. sympodialis allergen Mala s 1 is localized mainly in the yeast cell wall and exposed on the cell surface. Interestingly, Mala s 1 does not exhibit any significant sequence homology to known proteins. Here we present the crystal structure of Mala s 1 determined by single-wavelength anomalous dispersion techniques using selenomethionine-substituted Mala s 1. Mala s 1 folds into a 6-fold beta-propeller, a novel fold among allergens. The putative active site of Mala s 1 overlaps structurally to putative active sites in potential homologues, Q4P4P8 and Tri 14, from the plant parasites Ustilago maydis and Gibberella zeae, respectively. This resemblance suggests that Mala s 1 and the parasite proteins may have similar functions. In addition, we show that Mala s 1 binds to the phosphoinositides (PI) PI(3)P, PI(4)P, and PI(5)P, lipids possibly playing a role in the localization of Mala s 1 to the cell surface. The crystal structure of Mala s 1 will provide insights into the role of this major allergen in the host-microbe interactions and induction of an allergic response in AE.

About this Structure

Full crystallographic information is available from OCA.

Reference

Crystal structure of the major Malassezia sympodialis allergen Mala s 1 reveals a beta-propeller fold: a novel fold among allergens., Vilhelmsson M, Zargari A, Crameri R, Rasool O, Achour A, Scheynius A, Hallberg BM, J Mol Biol. 2007 Jun 15;369(4):1079-86. Epub 2007 Apr 12. PMID:17481656 Page seeded by OCA on Sun May 4 12:41:24 2008

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