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Proc. Natl. Acad. Sci. USA
Vol. 94, pp. 7192-7197, July 1997
Biochemistry

Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site

(cystine knot / mutagenesis / receptor dimerization)

Yves A. Muller, Bing Li, Hans W. Christinger, James A. Wells, Brian C. Cunningham, and Abraham M. de Vos

Genentech, Inc., Department of Protein Engineering, 460 Point San Bruno Boulevard, South San Francisco, CA 94080

Communicated by Sung-Hou Kim, University of California, Berkeley, CA, April 10, 1997 (received for review February 10, 1997)

Vascular endothelial growth factor (VEGF) is a homodimeric member of the cystine knot family of growth factors, with limitedsequence homology to platelet-derived growth factor (PDGF) andtransforming growth factor beta 2 (TGF-beta ). We have determined itscrystal structure at a resolution of 2.5 Å, and identified itskinase domain receptor (KDR) binding site using mutational analysis.Overall, the VEGF monomer resembles that of PDGF, but its N-terminalsegment is helical rather than extended. The dimerization modeof VEGF is similar to that of PDGF and very different from thatof TGF-beta . Mutational analysis of VEGF reveals that symmetricalbinding sites for KDR are located at each pole of the VEGF homodimer.Each site contains two functional "hot spots" composed of bindingdeterminants presented across the subunit interface. The two mostimportant determinants are located within the largest hot spoton a short, three-stranded sheet that is conserved in PDGF andTGF-beta . Functional analysis of the binding epitopes for two receptor-blockingantibodies reveal different binding determinants near each ofthe KDR binding hot spots.


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Q. Tao, M. V. Backer, J. M. Backer, and B. I. Terman
Kinase Insert Domain Receptor (KDR) Extracellular Immunoglobulin-like Domains 4-7 Contain Structural Features That Block Receptor Dimerization and Vascular Endothelial Growth Factor-induced Signaling
J. Biol. Chem., June 8, 2001; 276(24): 21916 - 21923.
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