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Crystallization of the receptor binding domain of vascular endothelial growth factor

✍ Scribed by Christinger, Hans W.; Muller, Yves A.; Berleau, Lea T.; Keyt, Bruce A.; Cunningham, Brian C.; Ferrara, Napoleone; de Vos, Abraham M.

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 530 KB
Volume: 26
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199611)26:3<353::aid-prot9>3.0.co;2-e

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✦ Synopsis

Vascular endothelial growth factor (VEGF) is a potent angiogenic factor with a unique specificity for vascular endothelial cells. In addition to its role in vasculogenesis and embryonic angiogenesis, VEGF is implicated in pathologic neovascularization associated with tumors and diabetic retinopathy. Four different constructs of a short variant of VEGF sufficient for receptor binding were overexpressed in Escherichia coli, refolded, purified, and crystallized in five different space groups. In order to facilitate the production of heavy atom derivatives, single cysteine mutants were designed based on the crystal structure of platelet-derived growth factor. A construct consisting of residues 8 to 109 was crystallized in space group P2,, with cell parameters a = 55.6 A, b = 60.4 A, c = 77.7 A, p = 90.0", and four monomers in the asymmetric unit. Native and derivative data were collected for two of the cysteine mutants as well as for wild-type VEGF.

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The opinions and assertions contained herein are the expressed views of the authors and are not to be construed as official or reflecting the views of the Departments of the Army or Defense.