β-1 CHAIN AND ITS DOCKING STUDY WITH COLCHICINE ANALOGUES
Priyanka Sharma, Ambarish Sharan Vidyarthi · 2010
Present study involves the homology modeling of human tubulin β-1 chain(TUBB1) using known protein structure of common pig tubulin. Its 3-D st ructure was evaluated and validated using PROCHECK comprising 96.8% amino acid residues in favored and allowed region of Ramachandran plot. Stability of the structure was confirmed by the program ERRAT having the overall quality factor as 83.476 and Verify_3D result with 83.85% residues having 3D-1D score > 0.2. With the structure of TUBB1 generated, flexible docking was performed using GLIDE. Results indicate that among 123 colchicine analogues, CID 5370577 was found as best interacting with TUBB1 having lowest dope score of -6.45 . Particularly residues TYR208, SER172 and GLU181 of TUBB1 at bond length 2.272, 1.997 and 2.249 respectively form hydrogen bonds and showed strong nonbonding interaction with analogue (CID 5370577). Further the generation of different derivatives can be made by the modification in the moieties of CID 5370577. Th ese derivatives can be used to develop effective drugs against acute gouty arthritis as well as cancer.