Effect of mutation on aggregation propensity in homology model structures of syntaxin-3 from Homo sapiens.

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dc.contributor.authorMaheshwari, Amutha Selvaraj
dc.contributor.authorRajesh, Durairaj
dc.contributor.authorPadmanabhan, Parasuraman
dc.contributor.authorArchunan, Govindaraju
dc.date.accessioned2014-12-29T05:12:24Z
dc.date.available2014-12-29T05:12:24Z
dc.date.issued2014-10
dc.description.abstractPerception of molecular mechanism would provide potent additional knowledge on mammalian membrane proteins involved in causing diseases. In human, syntaxin-3 (STX3) is a significant apical targeting protein in the epithelial membrane and in exocytosis process; it also acts as a vesicle transporter by cellular receptor in neutrophils, which is crucial for protein trafficking event. Structurally, syntaxin-3 has hydrophobic domain at carboxyl terminus that directs itself to intra-cellular compartments. In addition, the experimental structure of STX3 is not available and no mutational study has been carried out with natural variants of proteins. Moreover, there is no evidence so far for the natural variant Val286 of STX3 causing any diseases. Hence, in the present study, analyses of residue-based properties of the homology model STX3 were carried out along with mutations at carboxyl terminus of STX3 by implementing protein engineering and in silico approaches. The model structure of STX3 was constructed adopting Modeller v9.11 and the aggregation propensity was analyzed with BioLuminate tool. The results showed that there was reduction in aggregation propensity with point mutation at Val286, instead of Ile, resulting into increasing the structural stability of STX3. In conclusion, the Ccap exposed residue would be a suitable position for further mutational studies, particularly with Val286 of STX3 in human. This approach could gainfully be applied to STX3 for efficient drug designing which would be a valuable target in the cancer treatment.en_US
dc.identifier.citationMaheshwari Amutha Selvaraj, Rajesh Durairaj, Padmanabhan Parasuraman, Archunan Govindaraju. Effect of mutation on aggregation propensity in homology model structures of syntaxin-3 from Homo sapiens. Indian Journal of Biochemistry & Biophysics. 2014 Oct; 51(5): 335-342.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/154261
dc.language.isoenen_US
dc.publisherNISCAIR CSIR India.en_US
dc.source.urihttps://nopr.niscair.res.in/handle/123456789/29889en_US
dc.subjectAggregation propensityen_US
dc.subjectCancer therapyen_US
dc.subjectDirected evolutionen_US
dc.subjectHomology modelingen_US
dc.subjectMembrane proteinen_US
dc.subjectSyntaxin-3en_US
dc.subject.meshComputer Simulation
dc.subject.meshHumans
dc.subject.meshModels, Chemical
dc.subject.meshModels, Genetics
dc.subject.meshModels, Molecular
dc.subject.meshMultiprotein Complexes --chemistry
dc.subject.meshMultiprotein Complexes --genetics
dc.subject.meshMultiprotein Complexes --ultrastructure
dc.subject.meshMutagenesis, Site-Directed
dc.subject.meshMutation --genetics
dc.subject.meshProtein Binding
dc.subject.meshProtein Conformation
dc.subject.meshProtein Folding
dc.subject.meshProtein Multimerization
dc.subject.meshQa-SNARE Proteins --chemistry
dc.subject.meshQa-SNARE Proteins --genetics
dc.subject.meshQa-SNARE Proteins --ultrastructure
dc.subject.meshSequence Homology, Amino Acid
dc.titleEffect of mutation on aggregation propensity in homology model structures of syntaxin-3 from Homo sapiens.en_US
dc.typeArticleen_US
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