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1slu

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[[Image:1slu.png|left|200px]]
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{{STRUCTURE_1slu| PDB=1slu | SCENE= }}
{{STRUCTURE_1slu| PDB=1slu | SCENE= }}
===RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN===
===RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN===
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{{ABSTRACT_PUBMED_8634241}}
{{ABSTRACT_PUBMED_8634241}}
==About this Structure==
==About this Structure==
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1SLU is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLU OCA].
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[[1slu]] is a 2 chain structure of [[Ecotin]] and [[Trypsin]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLU OCA].
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==See Also==
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*[[Ecotin|Ecotin]]
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*[[Trypsin|Trypsin]]
==Reference==
==Reference==
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<ref group="xtra">PMID:8634241</ref><references group="xtra"/>
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<ref group="xtra">PMID:008634241</ref><ref group="xtra">PMID:009215573</ref><ref group="xtra">PMID:011880627</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Protein engineering]]
[[Category: Protein engineering]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:06:06 2009''
 

Revision as of 21:36, 25 July 2012

Template:STRUCTURE 1slu

Contents

RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN

Template:ABSTRACT PUBMED 8634241

About this Structure

1slu is a 2 chain structure of Ecotin and Trypsin with sequence from Escherichia coli and Rattus norvegicus. Full crystallographic information is available from OCA.

See Also

Reference

  • Brinen LS, Willett WS, Craik CS, Fletterick RJ. X-ray structures of a designed binding site in trypsin show metal-dependent geometry. Biochemistry. 1996 May 14;35(19):5999-6009. PMID:8634241 doi:http://dx.doi.org/10.1021/bi9530200
  • Briand L, Chobert JM, Tauzin J, Declerck N, Leonil J, Molle D, Tran V, Haertle T. Regulation of trypsin activity by Cu2+ chelation of the substrate binding site. Protein Eng. 1997 May;10(5):551-60. PMID:9215573
  • Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099

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