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Modeling of the potential coiled-coil structure of snapin protein and its interaction with SNARE complex
Autism is a developmental disability causing learning and memory disorder. The heart of the search for a cure for this syndrome is the need to understand dendrite branch patterning, a process crucial for proper synaptic transmission. Due to the association of snapin with the SNARE complex and its ro...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics Publishing Group
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891699/ https://www.ncbi.nlm.nih.gov/pubmed/17597906 |
Sumario: | Autism is a developmental disability causing learning and memory disorder. The heart of the search for a cure for this syndrome is the need to understand dendrite branch patterning, a process crucial for proper synaptic transmission. Due to the association of snapin with the SNARE complex and its role in synaptic transmission it is reported as a potential drug target for autism therapies. We wish to impart the noesis of the 3D structure of the snapin protein, and in this chase we predict the native structure from its sequence of amino acid residues using the classical Comparative protein structure modeling methods. The predicted protein model can be of great assistance in understanding the structural insights, which is necessary to understand the protein function. Understanding the interactions between snapin and SNARE complex is crucial in studying its role in the neurotransmitter release process. We also presented a computational model that shows the interaction between the snapin and SNAP-25 protein, a part of the larger SNARE complex. |
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