View source for 2lpn


==Solution Structure of N-Terminal domain of human Conserved Dopamine Neurotrophic Factor (CDNF)==
<StructureSection load='2lpn' size='340' side='right'caption='[[2lpn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lpn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LPN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2lpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpn OCA], [https://pdbe.org/2lpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lpn RCSB], [https://www.ebi.ac.uk/pdbsum/2lpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lpn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDNF_HUMAN CDNF_HUMAN] Trophic factor for dopamine neurons. Prevents the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When administered after 6-OHDA-lesioning, restores the dopaminergic function and prevents the degeneration of dopaminergic neurons in substantia nigra (By similarity).
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== Publication Abstract from PubMed ==
Parkinson's disease (PD) is a neurodegenerative disorder that is caused by the death of midbrain dopaminergic neurons. Current therapies for PD do not halt the neurodegeneration nor repair the affected neurons. Therefore, search for novel neurotrophic factors (NTF) for midbrain dopaminergic neurons, which could be used in novel therapeutic approaches, is highly wanted. In 2007, a potent NTF for dopaminergic neurons was described as the conserved dopamine neurotrophic factor (CDNF). Single doses of this protein protect and restore dopaminergic neurons in experimental models of PD. CDNF has two domains; an N-terminal saposin-like domain, which may bind to membranes; and a presumably intrinsically unstructured C-terminal which contains an internal cysteine bridge in a CXXC motif similar to that of thiol/disulphide oxidoreductases and isomerases, and may thus reduce the endoplasmic reticulum stress caused by incorrectly folded proteins. We show for the first time the nuclear magnetic resonance assignment of N-terminal domain of recombinant CDNF (residues 1-105) by solution 2D and 3D NMR spectroscopy. We were able to obtain a nearly complete resonance assignment, which is the first step toward the solution structure determination of this neurotrophic factor.

(1)H-, (13)C- and (15)N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF).,Latge C, Cabral KM, Almeida MS, Foguel D Biomol NMR Assign. 2012 Apr 18. PMID:22528768<ref>PMID:22528768</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Almeida MS]]
[[Category: Cabral KMS]]
[[Category: Foguel D]]
[[Category: Latge C]]
[[Category: Pires JRM]]