Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A

Markovic-Mueller, Sandra and Stuttfeld, Edward and Asthana, Mayanka and Weinert, Tobias and Bliven, Spencer and Goldie, Kenneth N. and Kisko, Kaisa and Capitani, Guido and Ballmer-Hofer, Kurt. (2017) Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A. Structure, 25 (2). pp. 341-352.

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Official URL: https://edoc.unibas.ch/78547/

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Vascular endothelial growth factors (VEGFs) regulate blood and lymph vessel development upon activation of three receptor tyrosine kinases: VEGFR-1, -2, and -3. Partial structures of VEGFR/VEGF complexes based on single-particle electron microscopy, small-angle X-ray scattering, and X-ray crystallography revealed the location of VEGF binding and domain arrangement of individual receptor subdomains. Here, we describe the structure of the full-length VEGFR-1 extracellular domain in complex with VEGF-A at 4 Å resolution. We combined X-ray crystallography, single-particle electron microscopy, and molecular modeling for structure determination and validation. The structure reveals the molecular details of ligand-induced receptor dimerization, in particular of homotypic receptor interactions in immunoglobulin homology domains 4, 5, and 7. Functional analyses of ligand binding and receptor activation confirm the relevance of these homotypic contacts and identify them as potential therapeutic sites to allosterically inhibit VEGFR-1 activity.
Faculties and Departments:05 Faculty of Science
UniBasel Contributors:Goldie, Kenneth N.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cell Press
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:01 Oct 2020 09:08
Deposited On:01 Oct 2020 09:08

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