Abstract
The novel protein, Cannabinoid receptor interacting protein (CRIP) is encoded by Cnrip gene, and is found on chromosome number 2 in humans. CRIP1a can modulate CB1 receptor cellular localization and signal transduction. However the structural aspects of CRIP1a and its interaction with CB1 are unknown. Because no sequence or structural homology with other known proteins is currently available, an ab initio modeling approach for prediction CRIP1a structure has been used. The Molecular docking and molecular dynamics simulations have been used to investigate binding and relative stability between CB1 and CRIP1a. The results show compact structure of 12 beta sheets along with small helix and loops, which is supported by secondary structure data, Ramachandram plot, Aggregation analysis, and lesser number of high energy zones. Further the entire protein was refined by 10 ns MD simulation with Gromacs and the structural changes were observed which appear to be related with rearrangement of hydrogen bonds. Molecular docking with CB1 C-terminal peptide revealed binding pocket in CRIP1a. The relationship between Cannabinoid receptor isoform one (CB1) and CRIP1a play significant roles in addiction, diabetes, cardiovascular disease, neurodegenerative disorders and the pain management.Grant Support:NIH DA03690 and ICMR, India.
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