1r60
From Proteopedia
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{{Theoretical_model}} | {{Theoretical_model}} | ||
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| - | [[Image:1r60.png|left|200px]] | ||
{{STRUCTURE_1r60| PDB=1r60 | SCENE= }} | {{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}} | {{ABSTRACT_PUBMED_14609438}} | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:014609438</ref><references group="xtra"/> | + | <ref group="xtra">PMID:014609438</ref><references group="xtra"/><references/> |
[[Category: Dunn, B M]] | [[Category: Dunn, B M]] | ||
[[Category: Durell, S R]] | [[Category: Durell, S R]] | ||
Revision as of 09:48, 24 March 2013
| Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution. |
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
Categories: Dunn, B M | Durell, S R | Li, M | Oda, K | Oyama, H | Wlodawer, A
