2LPN
Solution Structure of N-Terminal domain of human Conserved Dopamine Neurotrophic Factor (CDNF)
Summary for 2LPN
| Entry DOI | 10.2210/pdb2lpn/pdb |
| Related | 2w50 |
| NMR Information | BMRB: 18269 |
| Descriptor | Cerebral dopamine neurotrophic factor (1 entity in total) |
| Functional Keywords | nerve growth factor, neurotrophic factor, intercellular signaling protein, nerve tissue protein, neuronal growth-associated, hormone |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: Q49AH0 |
| Total number of polymer chains | 1 |
| Total formula weight | 11964.95 |
| Authors | Latge, C.,Cabral, K.M.S.,Foguel, D.,Pires, J.R.M.,Almeida, M.S. (deposition date: 2012-02-15, release date: 2013-02-20, Last modification date: 2024-10-30) |
| Primary citation | Latge, C.,Cabral, K.M.,Almeida, M.S.,Foguel, D. (1)H-, (13)C- and (15)N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF). Biomol.Nmr Assign., 7:101-103, 2013 Cited by PubMed Abstract: 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. PubMed: 22528768DOI: 10.1007/s12104-012-9388-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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