Title of article :
Structure of the Neutrophil-activating Protein from Helicobacter pylori
Author/Authors :
Giuseppe Zanotti، نويسنده , , Elena Papinutto، نويسنده , , William G. Dundon، نويسنده , , Roberto Battistutta، نويسنده , , Michela Seveso، نويسنده , , Giuseppe Del Giudice، نويسنده , , Rino Rappuoli، نويسنده , , Cesare Montecucco، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2002
Pages :
6
From page :
125
To page :
130
Abstract :
Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An H. pylori protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes.
Keywords :
ferritins , crystal structure , neutrophil-activating protein , iron storage , Helicobacter pylori
Journal title :
Journal of Molecular Biology
Serial Year :
2002
Journal title :
Journal of Molecular Biology
Record number :
1242082
Link To Document :
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