2yp0

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-	'''Unreleased structure'''	+	{{STRUCTURE_2yp0| PDB=2yp0 | SCENE= }}
		+	===Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, crystallized with 2'-AMPS===
-	The entry 2yp0 is ON HOLD until Paper Publication	+	==Function==
		+	[[http://www.uniprot.org/uniprot/CN37_MOUSE CN37_MOUSE]] May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.<ref>PMID:22393399</ref>
-	Authors: Myllykoski, M., Raasakka, A., Lehtimaki, M., Han, H., Kursula, P.	+	==About this Structure==
		+	[[2yp0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YP0 OCA].
-	Description: Catalytic domain of mouse 2',3'-cyclic nucleotide 3'-phosphodiesterase, crystallized with 2'-AMPS	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: 2',3'-cyclic-nucleotide 3'-phosphodiesterase]]
		+	[[Category: Mus musculus]]
		+	[[Category: Han, H.]]
		+	[[Category: Kursula, P.]]
		+	[[Category: Lehtimaki, M.]]
		+	[[Category: Myllykoski, M.]]
		+	[[Category: Raasakka, A.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Myelin]]
		+	[[Category: Nervous system]]

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Revision as of 15:47, 10 July 2013

Template:STRUCTURE 2yp0

Contents 1 Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, crystallized with 2'-AMPS 2 Function 3 About this Structure 4 Reference

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, crystallized with 2'-AMPS

Function

[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 Structure

2yp0 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

1. ↑ 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