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1r60

From Proteopedia

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[[Image:1r60.png|left|200px]]
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{{STRUCTURE_1r60| PDB=1r60 | SCENE= }}
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===A HOMOLOGY-DERIVED MODEL OF HUMAN TRIPEPTIDYL-PEPTIDASE I (CLN2)===
===A HOMOLOGY-DERIVED MODEL OF HUMAN TRIPEPTIDYL-PEPTIDASE I (CLN2)===
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{{ABSTRACT_PUBMED_14609438}}
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==About this Structure==
 
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R60 OCA].
 
==Reference==
==Reference==
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<ref group="xtra">PMID:14609438</ref><references group="xtra"/>
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<ref group="xtra">PMID:014609438</ref><references group="xtra"/>
[[Category: Dunn, B M]]
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[[Category: Durell, S R]]
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[[Category: Oyama, H]]
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[[Category: Wlodawer, A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:36:50 2010''
 

Revision as of 09:04, 21 October 2012

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.
Image:1r60.png

Template:STRUCTURE 1r60

A HOMOLOGY-DERIVED MODEL OF HUMAN TRIPEPTIDYL-PEPTIDASE I (CLN2)

Template:ABSTRACT PUBMED 14609438

Reference

  • Wlodawer A, Durell SR, Li M, Oyama H, Oda K, Dunn BM. A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases. BMC Struct Biol. 2003 Nov 11;3:8. PMID:14609438 doi:10.1186/1472-6807-3-8

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