2ype: Difference between revisions
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{{STRUCTURE_2ype| PDB=2ype | SCENE= }} | {{STRUCTURE_2ype| PDB=2ype | SCENE= }} | ||
===Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3'- cyclic AMP=== | ===Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3'- cyclic AMP=== | ||
{{ABSTRACT_PUBMED_23831225}} | |||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
<references group="xtra"/><references/> | <ref group="xtra">PMID:023831225</ref><references group="xtra"/><references/> | ||
[[Category: 2',3'-cyclic-nucleotide 3'-phosphodiesterase]] | [[Category: 2',3'-cyclic-nucleotide 3'-phosphodiesterase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
Revision as of 07:32, 18 July 2013
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3'- cyclic AMPCatalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3'- cyclic AMP
Template:ABSTRACT PUBMED 23831225
FunctionFunction
[CN37_MOUSE] May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.[1]
About this StructureAbout this Structure
2ype is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Myllykoski M, Raasakka A, Lehtimaki M, Han H, Kursula I, Kursula P. Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family. J Mol Biol. 2013 Jul 2. pii: S0022-2836(13)00391-4. doi:, 10.1016/j.jmb.2013.06.012. PMID:23831225 doi:10.1016/j.jmb.2013.06.012
- ↑ Myllykoski M, Raasakka A, Han H, Kursula P. Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation. PLoS One. 2012;7(2):e32336. Epub 2012 Feb 29. PMID:22393399 doi:10.1371/journal.pone.0032336