Title : Structural determinants of growth factor binding and specificity by
VEGF receptor 2 2
Abstract :
- Vascular endothelial growth factors ( VEGFs ) regulate blood and lymph vessel formation through activation of three receptor tyrosine kinases, VEGFR-1, -2, and -3
- The extracellular domain of VEGF receptors consists of seven immunoglobulin homology domains , which, upon ligand binding, promote receptor dimerization
- Dimerization initiates transmembrane signaling, which activates the intracellular tyrosine kinase domain of the receptor
- VEGF-C stimulates lymphangiogenesis and contributes to pathological angiogenesis via VEGFR-3
- However, proteolytically processed VEGF-C also stimulates VEGFR-2 , the predominant transducer of signals required for physiological and pathological angiogenesis
- Here we present the crystal structure of VEGF-C bound to the VEGFR-2 high-affinity-binding site , which consists of immunoglobulin homology domains D2 and D3
- This structure reveals a symmetrical 22 complex, in which left-handed twisted receptor domains wrap around the 2-fold axis of VEGF-C
- In the VEGFs , receptor specificity is determined by an N-terminal alpha helix and three peptide loops
- Our structure shows that two of these loops in VEGF-C bind to VEGFR-2 subdomains D2 and D3, while one interacts primarily with D3
- Additionally, the N-terminal helix of VEGF-C interacts with D2, and the groove separating the two VEGF-C monomers binds to the D2/D3 linker
- VEGF-C, unlike VEGF-A, does not bind VEGFR-1
- We therefore created VEGFR-1 / VEGFR-2 chimeric proteins to further study receptor specificity
- This biochemical analysis, together with our structural data, defined VEGFR-2 residues critical for the binding of VEGF-A and VEGF-C
- Our results provide significant insights into the structural features that determine the high affinity and specificity of VEGF / VEGFR interactions
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
- 13. VEGFR-2, residues
- 2. VEGF receptors, domain
- 3. receptor, domain
- 6. VEGFR, site
- 7. receptor, domains
- 9. VEGFR-2, subdomains
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):