VEGF homology domain

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Alignment of the amino acid sequence of the VEGF homology domain of selected VEGFs. The eight cysteine ​​residues are highlighted in yellow and other 100% conserved amino acid residues are highlighted in orange.

The VHD homology domain is the central structural element that is common to all members of the VEGF family. The minimal version is approx. 100 amino acids long and has a characteristic arrangement of eight cysteine amino acid residues, namely: CX 22 CPXCVX 3 RCXGCCX 6 CX 33-35 CXC . Six of these cysteines combine with each other and form three disulfide bridges in the so-called cystine knot structure (two disulfide bridges form a ring through which the third disulfide bridge then leads). The two other cysteines also form disulfide bridges, but not with one another, but with the other cysteine ​​of another VEGF molecule. VEGFs are therefore usually antiparallel, covalent dimers . Although the intermolecular disulfide bridges are not necessary for the formation of a VEGF dimer, they increase the thermal stability of the molecule.

Individual evidence

  1. ↑ David IR Holmes, Ian Zachary: The vascular endothelial growth factor (VEGF) family: angiogenic factors in health and disease . In: Genome Biology . 6, No. 2, 2005, p. 209. doi : 10.1186 / gb-2005-6-2-209 . PMID 15693956 . PMC 551528 (free full text).
  2. ↑ Ursula A. Vitt, Sheau Y. Hsu, Aaron JW Hsueh: Evolution and Classification of Cystine Knot-Containing Hormones and Related Extracellular Signaling Molecules . In: Molecular Endocrinology . 15, No. 5, May 1, 2001, pp. 681-694. doi : 10.1210 / mend.15.5.0639 . Retrieved March 24, 2017.
  3. ↑ Yves A. Muller, Christoph Heiring, Rolf Misselwitz, Karin Welfle, Heinz Welfle: The Cystine Knot Promotes Folding and Not Thermodynamic Stability in Vascular Endothelial Growth Factor . In: Journal of Biological Chemistry . 277, No. 45, November 8, 2002, pp. 43410-43416. doi : 10.1074 / jbc.M206438200 . PMID 12207021 . Retrieved April 18, 2019.