Huntington's disorder (HD), caused by mutations of the IT-15 gene, is an 
autosomal genetic disease that causes the breakdown of the nerve cells in the 
brain. The IT-15 gene encodes the huntingtin (Htt) protein. Htt, along with its 
interacting partners, are involved in maintaining proper communication among 
neurons. Our work is based on the interaction behavior between Htt (in three 
polyglutamine (polyQ) states that is Htt 0Q, 17Q and 36Q) and SH3GL3 interacting 
protein by using computational methods. We used the HADDOCK docking platform to 
find out the extent of interaction between Htt polyQ models and SH3GL3. The 
Htt36Q (mutated) showed higher interaction than Htt17Q (native) with SH3GL3. 
Molecular dynamics simulation was performed to uncover the structural 
fluctuations of polyQ models and their complexes. RMSD, Rg, SASA, and total 
interaction energy graph showed significant results, where as mutant Htt showed 
higher fluctuations and flexibility than native Htt. The increase in the length 
of polyQ was found to affect the stability, flexibility, and compactness of the 
protein and its complex. Our research provided a propitious approach to 
understand the consequence of polyglutamination in Htt and its relation with HD.