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| | ==Solution structure of catalytic domain of rat 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) protein== | | ==Solution structure of catalytic domain of rat 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) protein== |
| - | <StructureSection load='2ilx' size='340' side='right' caption='[[2ilx]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2ilx' size='340' side='right'caption='[[2ilx]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ilx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n4t 1n4t]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ILX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ilx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n4t 1n4t]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ILX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1woj|1woj]], [[2i3e|2i3e]], [[1n4t|1n4t]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2',3'-cyclic-nucleotide_3'-phosphodiesterase 2',3'-cyclic-nucleotide 3'-phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.37 3.1.4.37] </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=2ilx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilx OCA], [https://pdbe.org/2ilx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ilx RCSB], [https://www.ebi.ac.uk/pdbsum/2ilx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ilx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ilx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilx OCA], [http://pdbe.org/2ilx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ilx RCSB], [http://www.ebi.ac.uk/pdbsum/2ilx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ilx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CN37_RAT CN37_RAT]] May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). | + | [https://www.uniprot.org/uniprot/CN37_RAT CN37_RAT] May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphodiesterase|Phosphodiesterase]] | + | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2',3'-cyclic-nucleotide 3'-phosphodiesterase]] | + | [[Category: Large Structures]] |
| - | [[Category: Buffalo rat]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Denisov, A Y]] | + | [[Category: Denisov AY]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Kozlov, G]] | + | [[Category: Kozlov G]] |
| - | [[Category: Cnp]]
| + | |
| - | [[Category: Cnpase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nervous system]]
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| Structural highlights
Function
CN37_RAT May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Regeneration-induced CNPase homolog (RICH) is an axonal growth-associated protein, which is induced in teleost fish upon optical nerve injury. RICH consists of a highly acidic N-terminal domain, a catalytic domain with 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) activity and a C-terminal isoprenylation site. In vitro RICH and mammalian brain CNPase specifically catalyze the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides, but the physiologically relevant in vivo substrate remains unknown. Here, we report the NMR structure of the catalytic domain of goldfish RICH and describe its binding to CNPase inhibitors. The structure consists of a twisted nine-stranded antiparallel beta-sheet surrounded by alpha-helices on both sides. Despite significant local differences mostly arising from a seven-residue insert in the RICH sequence, the active site region is highly similar to that of human CNPase. Likewise, refinement of the catalytic domain of rat CNPase using residual dipolar couplings gave improved agreement with the published crystal structure. NMR titrations of RICH with inhibitors point to a similar catalytic mechanism for RICH and CNPase. The results suggest a functional importance for the evolutionarily conserved phosphodiesterase activity and hint of a link with pre-tRNA splicing.
Solution structure of the catalytic domain of RICH protein from goldfish.,Kozlov G, Denisov AY, Pomerantseva E, Gravel M, Braun PE, Gehring K FEBS J. 2007 Mar;274(6):1600-9. PMID:17480208[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kozlov G, Denisov AY, Pomerantseva E, Gravel M, Braun PE, Gehring K. Solution structure of the catalytic domain of RICH protein from goldfish. FEBS J. 2007 Mar;274(6):1600-9. PMID:17480208 doi:10.1111/j.1742-4658.2007.05707.x
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