Fig. 3 | Signal Transduction and Targeted Therapy

Fig. 3

From: Vascular endothelial growth factor signaling in health and disease: from molecular mechanisms to therapeutic perspectives

Fig. 3

Structural domains of vascular endothelial growth factor receptors (VEGFRs) and isoforms of soluble VEGFR1. a Domain organization of VEGFR1, VEGFR2, and VEGFR3. Each receptor has key structural features, including Ig-like extracellular domains (D1-D7), transmembrane domain (TMD), juxtamembrane domain (JMD), kinase domain (KD), and C-terminal domain (CTD). b Alternative splicing generates five distinct splice variants of VEGFR1: the full-length VEGFR1, VEGFR1 with intron 13 retention (sVEGFR1-i13), VEGFR1 with intron 14 retention (sVEGFR1-i14), and the soluble isoforms sVEGFR1-e15a and sVEGFR1-e15b with alternative terminal exons. The schematic highlights the differences in domain configurations between full-length receptors and their soluble forms, illustrating the structural diversity resulting from alternative splicing. Created in BioRendender.com

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