2oxz

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[[Image:2oxz.png|left|200px]]
[[Image:2oxz.png|left|200px]]
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{{STRUCTURE_2oxz| PDB=2oxz | SCENE= }}
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==About this Structure==
==About this Structure==
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2OXZ is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXZ OCA].
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[[2oxz]] is a 3 chain structure of [[Elastase]] and [[Matrix metalloproteinase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXZ OCA].
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==See Also==
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*[[Elastase|Elastase]]
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*[[Matrix metalloproteinase|Matrix metalloproteinase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:17096442</ref><references group="xtra"/>
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<ref group="xtra">PMID:017096442</ref><ref group="xtra">PMID:018156340</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Macrophage elastase]]
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[[Category: Maletta, M.]]
[[Category: Maletta, M.]]
[[Category: Yeo, K J.]]
[[Category: Yeo, K J.]]
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[[Category: Hydrolase]]
[[Category: Matrix metalloproteinase]]
[[Category: Matrix metalloproteinase]]
[[Category: Mmp-12]]
[[Category: Mmp-12]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:54:41 2009''
 

Revision as of 12:05, 26 July 2012

Template:STRUCTURE 2oxz

Contents

Human MMP-12 in complex with two peptides PQG and IAG

About this Structure

2oxz is a 3 chain structure of Elastase and Matrix metalloproteinase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Bertini I, Calderone V, Fragai M, Luchinat C, Maletta M, Yeo KJ. Snapshots of the reaction mechanism of matrix metalloproteinases. Angew Chem Int Ed Engl. 2006 Dec 4;45(47):7952-5. PMID:17096442 doi:10.1002/anie.200603100
  • Xiao Z, Bergeron H, Grosse S, Beauchemin M, Garron ML, Shaya D, Sulea T, Cygler M, Lau PC. Improvement of the thermostability and activity of a pectate lyase by single amino acid substitutions, using a strategy based on melting-temperature-guided sequence alignment. Appl Environ Microbiol. 2008 Feb;74(4):1183-9. Epub 2007 Dec 21. PMID:18156340 doi:http://dx.doi.org/10.1128/AEM.02220-07

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