Abstract
Introduction Fragile X syndrome (FXS) is one of the most common inherited forms of intellectual disability (ID).1,2 It happens because of expansion of CGG repeat sequence in the first exon of the FMR1 gene, gives rise to transcriptional silencing of the gene and resultant low or absence of gene p
Highlights
Fragile X syndrome (FXS) is one of the most common inherited forms of intellectual disability (ID)[1,2]
On the other hand, mutated fragile X mental retardation protein (FMRP) (m) protein was modeled as predicted structure by using 2KBD as a template so that any change in the amino acid position brought by mutation could be detected as altered structure
CYF1P1 and CYF2P2 protein found common structural homolog as PDBID 3P8C_A encoding Cytoplasmic FMR1interacting protein 1 of H. sapiens; FIP protein showed homology with Uricase enzyme having PDB ID code 2YZB expressing in Arthrobacter globiformis; Tudor domain-containing protein3 (TDRD3) protein found template homolog with PDB
Summary
Fragile X syndrome (FXS) is one of the most common inherited forms of intellectual disability (ID)[1,2]. It happens because of expansion of CGG repeat sequence in the first exon of the FMR1 gene, gives rise to transcriptional silencing of the gene and resultant low or absence of gene product, fragile X mental retardation protein (FMRP)[3].The protein involves in proper synaptic plasticity, neuronal morphology, and cognitive development and down regulation leads to different levels of ID4. By using Bioinformatics approach, model experimentally determined protein structures are primarily used in the docking and interaction studies These stable protein structures could be used by involving docking specific algorithms those have.
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