2r28
From Proteopedia
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[[Image:2r28.png|left|200px]] | [[Image:2r28.png|left|200px]] | ||
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{{STRUCTURE_2r28| PDB=2r28 | SCENE= }} | {{STRUCTURE_2r28| PDB=2r28 | SCENE= }} | ||
===The complex Structure of Calmodulin Bound to a Calcineurin Peptide=== | ===The complex Structure of Calmodulin Bound to a Calcineurin Peptide=== | ||
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{{ABSTRACT_PUBMED_18384083}} | {{ABSTRACT_PUBMED_18384083}} | ||
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==See Also== | ==See Also== | ||
- | *[[Calmodulin]] | + | *[[Calmodulin|Calmodulin]] |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:018384083</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphoprotein phosphatase]] | [[Category: Phosphoprotein phosphatase]] | ||
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[[Category: Ye, Q.]] | [[Category: Ye, Q.]] | ||
[[Category: Zheng, J.]] | [[Category: Zheng, J.]] | ||
- | [[Category: Acetylation]] | ||
- | [[Category: Alternative splicing]] | ||
- | [[Category: Calcium]] | ||
[[Category: Calmodulin-binding]] | [[Category: Calmodulin-binding]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Iron]] | [[Category: Iron]] | ||
- | [[Category: Metal binding protein | + | [[Category: Metal binding protein-hydrolase complex]] |
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Methylation]] | [[Category: Methylation]] | ||
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[[Category: Protein phosphatase]] | [[Category: Protein phosphatase]] | ||
[[Category: Protein-peptide complex]] | [[Category: Protein-peptide complex]] | ||
- | [[Category: Ubl conjugation]] | ||
- | [[Category: Zinc]] |
Revision as of 23:30, 26 July 2012
Contents |
The complex Structure of Calmodulin Bound to a Calcineurin Peptide
Template:ABSTRACT PUBMED 18384083
About this Structure
2r28 is a 4 chain structure of Calmodulin with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Ye Q, Wang H, Zheng J, Wei Q, Jia Z. The complex structure of calmodulin bound to a calcineurin peptide. Proteins. 2008 Apr 2;. PMID:18384083 doi:10.1002/prot.22032