Title : The RGD finger of
Del-1 is a unique structural feature critical for integrin binding
Abstract :
- Developmental endothelial cell locus-1 ( Del-1 ) glycoprotein is secreted by endothelial cells and a subset of macrophages
- Del-1 plays a regulatory role in vascular remodeling and functions in innate immunity through interaction with integrin α(V)β(3)
- Del-1 contains 3 epidermal growth factor (EGF)-like repeats and 2 discoidin-like domains
- An Arg-Gly-Asp (RGD) motif in the second EGF domain (EGF2) mediates adhesion by endothelial cells and phagocytes
- We report the crystal structure of its 3 EGF domains
- The RGD motif of EGF2 forms a type II' β turn at the tip of a long protruding loop, dubbed the RGD finger
- Whereas EGF2 and EGF3 constitute a rigid rod via an interdomain calcium ion binding site , the long linker between EGF1 and EGF2 lends considerable flexibility to EGF1
- Two unique O-linked glycans and 1 N-linked glycan locate to the opposite side of EGF2 from the RGD motif
- These structural features favor integrin binding of the RGD finger
- Mutagenesis data confirm the importance of having the RGD motif at the tip of the RGD finger
- A database search for EGF domain sequences shows that this RGD finger is likely an evolutionary insertion and unique to the EGF domain of Del-1 and its homologue milk fat globule- EGF 8
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycoprotein, , glycoprotein, -, -
- 3. contains, , Del-1, 3 epidermal growth factor (EGF)-like repeats, -
Output(Part-Of) (sent_index,
protein,
site):
- 11. Del-1, domain
- 11. EGF 8, domain
- 11. EGF, domain
- 11. EGF, sequences
- 3. Del-1, domains
- 4. -, domain
- 4. EGF, domain
- 5. 3 EGF, domains
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):