2ydd: Difference between revisions
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<StructureSection load='2ydd' size='340' side='right'caption='[[2ydd]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2ydd' size='340' side='right'caption='[[2ydd]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ydd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2ydd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AM:ADENOSINE-2-MONOPHOSPHATE'>2AM</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ydd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydd OCA], [https://pdbe.org/2ydd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydd RCSB], [https://www.ebi.ac.uk/pdbsum/2ydd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydd ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ydd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydd OCA], [https://pdbe.org/2ydd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydd RCSB], [https://www.ebi.ac.uk/pdbsum/2ydd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Kursula | [[Category: Kursula P]] | ||
[[Category: Myllykoski | [[Category: Myllykoski M]] | ||
Latest revision as of 11:12, 23 August 2023
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, soaked with 2',3'-cyclic AMPCatalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, soaked with 2',3'-cyclic AMP
Structural highlights
FunctionCN37_MOUSE May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.[1] Publication Abstract from PubMedThe 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) is a highly abundant membrane-associated enzyme in the myelin sheath of the vertebrate nervous system. CNPase is a member of the 2H phosphoesterase family and catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates; however, its physiological substrate and function remain unknown. It is likely that CNPase participates in RNA metabolism in the myelinating cell. We solved crystal structures of the phosphodiesterase domain of mouse CNPase, showing the binding mode of nucleotide ligands in the active site. The binding mode of the product 2'-AMP provides a detailed view of the reaction mechanism. Comparisons of CNPase crystal structures highlight flexible loops, which could play roles in substrate recognition; large differences in the active-site vicinity are observed when comparing more distant members of the 2H family. We also studied the full-length CNPase, showing its N-terminal domain is involved in RNA binding and dimerization. Our results provide a detailed picture of the CNPase active site during its catalytic cycle, and suggest a specific function for the previously uncharacterized N-terminal domain. Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: active-site ligand binding and molecular conformation.,Myllykoski M, Raasakka A, Han H, Kursula P PLoS One. 2012;7(2):e32336. Epub 2012 Feb 29. PMID:22393399[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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