2xs3: Difference between revisions

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[[Image:2xs3.png|left|200px]]
[[Image:2xs3.png|left|200px]]


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{{STRUCTURE_2xs3|  PDB=2xs3  |  SCENE=  }}  
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===STRUCTURE OF KARILYSIN CATALYTIC MMP DOMAIN===
===STRUCTURE OF KARILYSIN CATALYTIC MMP DOMAIN===


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{{ABSTRACT_PUBMED_21166898}}
{{ABSTRACT_PUBMED_21166898}}


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==Reference==
==Reference==
<ref group="xtra">PMID:21166898</ref><ref group="xtra">PMID:19919176</ref><ref group="xtra">PMID:20375548</ref><references group="xtra"/>
<ref group="xtra">PMID:021166898</ref><ref group="xtra">PMID:019919176</ref><ref group="xtra">PMID:020375548</ref><references group="xtra"/>
[[Category: Synthetic construct]]
[[Category: Synthetic construct]]
[[Category: Tannerella forsythia]]
[[Category: Tannerella forsythia]]

Revision as of 18:31, 7 January 2013

File:2xs3.png

Template:STRUCTURE 2xs3

STRUCTURE OF KARILYSIN CATALYTIC MMP DOMAIN

Template:ABSTRACT PUBMED 21166898

About this Structure

2xs3 is a 4 chain structure with sequence from Tannerella forsythia and Synthetic construct. Full crystallographic information is available from OCA.

Reference

  1. Cerda-Costa N, Guevara T, Karim AY, Ksiazek M, Nguyen KA, Arolas JL, Potempa J, Gomis-Ruth FX. The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases. Mol Microbiol. 2011 Jan;79(1):119-132. doi:, 10.1111/j.1365-2958.2010.07434.x. Epub 2010 Nov 2. PMID:21166898 doi:10.1111/j.1365-2958.2010.07434.x
  2. Karim AY, Kulczycka M, Kantyka T, Dubin G, Jabaiah A, Daugherty PS, Thogersen IB, Enghild JJ, Nguyen KA, Potempa J. A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. Biol Chem. 2010 Jan;391(1):105-17. PMID:19919176 doi:10.1515/BC.2010.009
  3. Koziel J, Karim AY, Przybyszewska K, Ksiazek M, Rapala-Kozik M, Nguyen KA, Potempa J. Proteolytic inactivation of LL-37 by karilysin, a novel virulence mechanism of Tannerella forsythia. J Innate Immun. 2010;2(3):288-93. Epub 2010 Feb 4. PMID:20375548 doi:10.1159/000281881

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