1r60: Difference between revisions

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'''Theoretical Model'''
{{Theoretical_model}}
{{Seed}}
[[Image:1r60.png|left|200px]]


The entry 1R60 is a Theoretical Model titled 'A homology-derived model of human tripeptidyl-peptidase I (CLN2)'.
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[[Category:Theoretical Model]]
===A HOMOLOGY-DERIVED MODEL OF HUMAN TRIPEPTIDYL-PEPTIDASE I (CLN2)===




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==About this Structure==
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R60 OCA].
 
==Reference==
<ref group="xtra">PMID:14609438</ref><references group="xtra"/>
[[Category: Dunn, B M]]
[[Category: Durell, S R]]
[[Category: Li, M]]
[[Category: Oda, K]]
[[Category: Oyama, H]]
[[Category: Wlodawer, A]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:36:50 2010''

Revision as of 04:36, 8 April 2010

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

Template:STRUCTURE 1r60

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

Template:ABSTRACT PUBMED 14609438

About this Structure

Full crystallographic information is available from OCA.

Reference

  1. 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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