Endorepellin binds KDR (VEGFR2)

Stable Identifier
R-HSA-4088281
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

Endorepellin is the C-terminal domain V of perlecan, constituting amino acids 3687?4391 (Mongiat et al. 2004). It has anti-angiogenic properties, blocking endothelial cell adhesion to fibronectin and type I collagen (Mongiat et al. 2003). Endorepellin and a smaller fragement constituting the third laminin G?like (LG) domain (LG3) disrupt actin stress fibers and focal adhesions via an interaction with the collagen receptor alpha2beta1 integrin (Bix et al. 2004). The first and second laminin G domains 1 of endorepellin bind specifically and with high affinity to Ig domains 3?5 of VEGFR2 (Willis et al. 2013).

Literature References
Participants
Participant Of
Orthologous Events
Authored
Reviewed