N-terminal subrepeat of tandem repeat unit 6 of reelin and related proteins
Reelin is an extracellular glycoprotein involved in neuronal development, specifically in the brain cortex. It contains 8 tandemly repeated units, each of which is composed of two highly similar subrepeats and a central EGF domain. This model characterizes the N-terminal subrepeat, which directly contacts the C-terminal subrepeat and the EGF domain in a compact arrangement. Consecutive reelin repeat units are packed together to form an overall rod-like molecular structure. Reelin repeats 5 and 6 are reported to interact with neuronal receptors, the apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), triggering a signaling cascade upon binding and subsequent tyrosine phosphorylation of the cytoplasmic disabled-1 (Dab1).
Comment:Low-density lipoprotein receptor (LDLR) consists of 3 types of protein modules: LDLR class A (LA), epidermal growth factor (EGF) and YWTD beta-propeller; it recognizes reelin protein through its LA module.
Structure:3A7Q: Mouse reelin repeats 5 and 6 bind low-density lipoprotein receptor-related protein 8; contacts at 4.0A
Jiyao W et al.(2023). "The conserved domain database in 2023.",