In molecular biology, the BPS domain (Between PH and SH2) domain is a protein domain of approximately 45 amino acids found in the adaptor proteins Grb7/|Grb10/Grb14. It mediates inhibition of the tyrosine kinase domain of the insulin receptor by binding of the N-terminal portion of the BPS domain to the substrate peptide groove of the kinase, acting as a pseudosubstrate inhibitor. It is composed of two beta strands and a C-terminal helix.[1]
| BPS | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the grb14 bps region in complex with the insulin receptor tyrosine kinase | |||||||||
| Identifiers | |||||||||
| Symbol | BPS | ||||||||
| Pfam | PF08947 | ||||||||
| InterPro | IPR015042 | ||||||||
| |||||||||
References
edit- ^ Depetris RS, Hu J, Gimpelevich I, Holt LJ, Daly RJ, Hubbard SR (October 2005). "Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14". Mol. Cell. 20 (2): 325–33. doi:10.1016/j.molcel.2005.09.001. PMC 4526137. PMID 16246733.
 | This protein-related article is a stub. You can help Wikipedia by expanding it. |