1of9: Difference between revisions

Revision as of 17:12, 28 July 2008

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File:1of9.png

Template:STRUCTURE 1of9

SOLUTION STRUCTURE OF THE PORE FORMING TOXIN OF ENTAMOEBA HISTOLYTICA (AMOEBAPORE A)SOLUTION STRUCTURE OF THE PORE FORMING TOXIN OF ENTAMOEBA HISTOLYTICA (AMOEBAPORE A)

Template:ABSTRACT PUBMED 14970207

About this StructureAbout this Structure

1OF9 is a Single protein structure of sequence from Entamoeba histolytica. Full experimental information is available from OCA.

ReferenceReference

Solution structure of the pore-forming protein of Entamoeba histolytica., Hecht O, Van Nuland NA, Schleinkofer K, Dingley AJ, Bruhn H, Leippe M, Grotzinger J, J Biol Chem. 2004 Apr 23;279(17):17834-41. Epub 2004 Feb 17. PMID:14970207

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''SOLUTION STRUCTURE OF THE PORE FORMING TOXIN OF ENTAMOEBA HISTOLYTICA (AMOEBAPORE A)'''
+===SOLUTION STRUCTURE OF THE PORE FORMING TOXIN OF ENTAMOEBA HISTOLYTICA (AMOEBAPORE A)===
-==Overview==
+<!--
-Amoebapore A is a 77-residue protein from the protozoan parasite and human pathogen Entamoeba histolytica. Amoebapores lyse both bacteria and eukaryotic cells by pore formation and play a pivotal role in the destruction of host tissues during amoebiasis, one of the most life-threatening parasitic diseases. Amoebapore A belongs to the superfamily of saposin-like proteins that are characterized by a conserved disulfide bond pattern and a fold consisting of five helices. Membrane-permeabilizing effector molecules of mammalian lymphocytes such as porcine NK-lysin and the human granulysin share these structural attributes. Several mechanisms have been proposed to explain how saposin-like proteins form membrane pores. All mechanisms indicate that the surface charge distribution of these proteins is the basis of their membrane binding capacity and pore formation. Here, we have solved the structure of amoebapore A by NMR spectroscopy. We demonstrate that the specific activation step of amoebapore A depends on a pH-dependent dimerization event and is modulated by a surface-exposed histidine residue. Thus, histidine-mediated dimerization is the molecular switch for pore formation and reveals a novel activation mechanism of pore-forming toxins.
+The line below this paragraph, {{ABSTRACT_PUBMED_14970207}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14970207 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14970207}}
 ==About this Structure==
-OF9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OF9 OCA].
+OF9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OF9 OCA].
 ==Reference==
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 [[Category: Saplip]]
 [[Category: Toxin]]
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