Related Experiment Video

Updated: Jul 26, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

12.7K

Structural insight into CD93 recognition by IGFBP7

Yueming Xu, Yi Sun, Yuwen Zhu

    Biorxiv : the Preprint Server for Biology
    |June 19, 2023
    PubMed

    Insights

    This study reveals the structural basis of the CD93-IGFBP7 interaction, crucial for endothelial cell (EC) angiogenesis and tumor vascularization. Understanding this interaction aids in developing targeted therapies for cancer by disrupting tumor microenvironment signaling.

    Area of Science:

    • Molecular and Cellular Biology
    • Cancer Biology
    • Structural Biology

    Background:

    • The CD93/IGFBP7 axis is critical for endothelial cell (EC) angiogenesis and migration, with upregulation contributing to tumor vascular abnormalities.
    • Blocking the CD93-IGFBP7 interaction can create a therapeutic tumor microenvironment, but the precise mechanism of their association is unknown.

    Approach:

    • Determined the crystal structure of the human CD93-IGFBP7 complex, focusing on the interaction between CD93's EGF1 domain and IGFBP7's IB domain.
    • Utilized mutagenesis studies to confirm the binding interactions and specificities between CD93 and IGFBP7.
    • Conducted cellular and mouse tumor studies to validate the physiological relevance of the CD93-IGFBP7 interaction in EC angiogenesis.

    Key Points:

    • Elucidated the structural basis of CD93-IGFBP7 complex formation, identifying specific interaction domains.
    • Confirmed the functional significance of the CD93-IGFBP7 interaction in EC angiogenesis through in vitro and in vivo experiments.
    • Provided insights into the cell surface architecture of CD93 and its role as a platform for ligand binding.

    Conclusions:

    • The CD93-IGFBP7 interaction is a key driver of EC angiogenesis and tumor vascularization.
    • Structural and functional data provide a foundation for developing targeted therapeutic agents to disrupt CD93-IGFBP7 signaling in the tumor microenvironment.
    • Understanding CD93's architecture offers new perspectives on cell surface interactions and signaling pathways.

    More Related Videos

    Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex07:17

    Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex

    Published on: August 2, 2021

    2.6K
    Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization08:57

    Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization

    Published on: October 6, 2019

    10.0K

    Related Concept Videos

    T Cell Activation and Clonal Selection01:22

    T Cell Activation and Clonal Selection

    T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
    Naive T cells that have not yet encountered an antigen express two primary CD...
    837
    Receptor Downregulation in MVBs01:15

    Receptor Downregulation in MVBs

    Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
    The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
    2.1K
    Immunoglobulin-like Cell Adhesion Molecules01:31

    Immunoglobulin-like Cell Adhesion Molecules

    Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
    Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
    3.3K
    TGF - β Signaling Pathway01:16

    TGF - β Signaling Pathway

    The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
    7.5K