Welocome to the Vascular Endothelial Growth Factor Tutorial. This tutorial was made as a student webpage for Dr. Campbell's Molecular Biology class at Davidson College.



Reset Chime Image .

Click here to see a monomer of VEGF.
Look at the two chains that compose the most basic form of functional VEGF dimer. Click here.

Often homodimers bind together to form more complex VEGF structures. Click the button below to see two homodimers bound together.

Click the buttons below to see how the chains enteract with each other.
Chain A:
Chain B:
Chain C:
Chain D:

Each monomer possesses six beta sheets shown here in red. .
The two monomers that form functional VEGF run antiparallel and are held together by disulfide bonds shown here in red

The central feature in each monomer is the cystine knot motif that consists of an eight ring structure formed by cystine residues and disulfide bonds. Let's look now at the cystine residues in blue. .

Notice how the three disulfide bonds interact with the cystine residues on one strand (in blue) forming the cystine knot motif, and how the fourth disulfide bond interacts with a cystine (in cyan) on the opposite antiparallel chain to bind it together. This particular motif forms the receptor binding domain of the VEGF protein.

Secondary structures of VEGF are formed by hydrogen bonds. You can view the H bonds by clicking on the follown button, where they are displayed in red.

As stated above there are seven beta sheets in VEGF, that are held together by Hydrogen bonds. Notice that the number of H-bonds varies between the different beta sheets. Between B3 and B5 there is only one hydrogen bond making the sheets very irregular. .

REFRENCES

Joukov, V., Kaipainen, A., Jeltsch, M. (1997).Vascular Endothelial Growth Factors VEGF-B and VEGF-C. Journal of Cellular Physiology 1997; 173 211-125.

Shinkaruk S, Bayle M, Lain G, Deleris G. (2003) Vascular Endothelial Growth Factor and Emerging Target for Cancer Chemotherapy. Curr Med Chem Anti-Canc Agents 2003 Mar;3(2):95-117

Muller, Y.A., Christinger, H.W., Keyt, B.A., de Vos, A.M.,. (1997). The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 Å resolution: multiple copy flexibility and receptor binding.
Structure 1997, 5:1325-1338.

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