In:
Peptide Science, Wiley, Vol. 94, No. 6 ( 2010-01), p. 800-809
Abstract:
Vascular endothelial growth factor (VEGF) is a potent angiogenic factor. Its biological activity is mediated by the binding to the extracellular domain of two tyrosine kinase transmembrane receptors: VEGFR1 and VEGFR2. Deletion studies showed that VEGF binding site resides in the first three domains of VEGFR1 and in domains 2 and 3 of VEGFR2. In particular, the second extracellular domain of VEGFR1 (VEGFR1 D2 ) contains most of the VEGF binding requirements. Here, we report an efficient expression protocol and the molecular characterization by spectroscopic techniques of VEGFR1 D2 . The protein was expressed in E. coli and refolded from inclusion bodies. The recombinant protein assumes the correct fold as assessed by a combination of biochemical and functional assays as well as by NMR characterization. Furthermore, the recombinant VEGFR1 D2 was analyzed by circular dichroism and fluorescence spectroscopy. The protein obtained by this procedure is suitable for the structural characterization of the complexes with receptor binders and to be used in interaction/screening studies. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 800–809, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Type of Medium:
Online Resource
ISSN:
0006-3525
Language:
English
Publisher:
Wiley
Publication Date:
2010
detail.hit.zdb_id:
2159538-0
detail.hit.zdb_id:
1480801-8
SSG:
12
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