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Computational analysis and functional prediction of ubiquitin hypothetical protein: A possible target in parkinson disease

dc.contributor.authorBarragán-Osorio L.
dc.contributor.authorGiraldo G.
dc.contributor.authorAlméciga-Diaz C.J.
dc.contributor.authorAliev G.
dc.contributor.authorBarreto G.E.
dc.contributor.authorGonzalez J.
dc.date.accessioned2020-09-02T22:12:59Z
dc.date.available2020-09-02T22:12:59Z
dc.date.issued2016
dc.identifier10.2174/1871524915666150722120605
dc.identifier.citation16, 1, 4-11
dc.identifier.issn18715249
dc.identifier.urihttps://hdl.handle.net/20.500.12728/3686
dc.descriptionParkinson´s disease (PD) is a high prevalent progressive neurodegenerative disorder characterized by degeneration of dopaminergic neurons and intracytoplasmatic aggregation of α-synuclein called Lewy Bodies. Anomalies in the proteasomal and endosomal ubiquitin related degradation of α-synuclein have been related with PD. Among the different proteins described in ubiquitin pathway, the hypothetical protein CAB55973.1 was identified previously. Here we modeled this hypothetical protein in order to contribute to the understanding of PD pathogenesis that should be served as an input in the future as drug targets. This study predicted a three-dimensional model of the complete sequence of hypothetical protein CAB55973.1 with a high value of identity and a good homology quality. Subcellular localization was found in the cytoplasm, mainly in the endosomal membrane. 36 protein-protein interactions related to PD were found. 11 residues were predicted to interact with target proteins for ubiquitination. Binding site prediction showed that one domain (residues 163 to 238) might be involved in ubiquitination of target proteins. In this ubiquitin domain, residues were distributed similarly to those of the binding site of the ubiquitin interacting with the UIM of Hrs protein (PDB 2D3G). The hypothetical protein was constructed based on the complete sequence alignment, which allowed predicting the structure with a high accuracy. The functional prediction showed that only one domain of the hypothetical protein might be involved in the α- synuclein ubiquitination of the endosomal pathway of the PD. © 2016 Bentham Science Publishers.
dc.language.isoen
dc.publisherBentham Science Publishers
dc.subjectHomology mathematical modeling
dc.subjectHypothetical protein
dc.subjectIn-silico
dc.subjectParkinson disease
dc.subjectUbiquitin
dc.subjectubiquitin
dc.subjectalpha synuclein
dc.subjectantiparkinson agent
dc.subjectubiquitin
dc.subjectArticle
dc.subjectgene mutation
dc.subjecthuman
dc.subjectmathematical model
dc.subjectParkinson disease
dc.subjectpeptide mapping
dc.subjectprotein analysis
dc.subjectprotein binding
dc.subjectprotein expression
dc.subjectprotein localization
dc.subjectprotein protein interaction
dc.subjectprotein secondary structure
dc.subjectprotein structure
dc.subjectproteomics
dc.subjectquality control
dc.subjectreliability
dc.subjectsequence alignment
dc.subjectsignal transduction
dc.subjectamino acid sequence
dc.subjectbinding site
dc.subjectbiology
dc.subjectcell fractionation
dc.subjectchemical structure
dc.subjectchemistry
dc.subjectdrug effects
dc.subjectgenetics
dc.subjectmolecular genetics
dc.subjectParkinson disease
dc.subjecttheoretical model
dc.subjectubiquitination
dc.subjectalpha-Synuclein
dc.subjectAmino Acid Sequence
dc.subjectAntiparkinson Agents
dc.subjectBinding Sites
dc.subjectComputational Biology
dc.subjectHumans
dc.subjectModels, Molecular
dc.subjectModels, Theoretical
dc.subjectMolecular Sequence Data
dc.subjectParkinson Disease
dc.subjectProtein Structure, Secondary
dc.subjectSubcellular Fractions
dc.subjectUbiquitination
dc.subjectUbiquitins
dc.titleComputational analysis and functional prediction of ubiquitin hypothetical protein: A possible target in parkinson disease
dc.typeArticle


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