|
Synonyms: vascular endothelial growth factor A | vascular permeability factor (VPF) | VEGF-A
Compound class:
Endogenous peptide in human, mouse or rat
Comment: The active peptide is anti-parallel homodimer linked by disulphide bonds. VEGFA exists as four isoforms of 121, 165, 189 and 206 amino acids. The shortest variant contains the full VEGFR2 binding site but lacks domains that are involved in interactions with extracellular-matrix and co-receptors which are present in the longer isoforms [14-15].
A recombinant single-chain derivative of VEGFA121 (scVEGF) can be used experimentally as a fully functional peptide that binds and activates VEGFR2 in the same manner as endogenous VEGFA [1]. scVEGF can be labelled with a single fluorophore at its N-terminal, for use as a molecular probe [3].
Species: Human
Ligand Activity Visualisation ChartsThese are box plot that provide a unique visualisation, summarising all the activity data for a ligand taken from ChEMBL and GtoPdb across multiple targets and species. Click on a plot to see the median, interquartile range, low and high data points. A value of zero indicates that no data are available. A separate chart is created for each target, and where possible the algorithm tries to merge ChEMBL and GtoPdb targets by matching them on name and UniProt accession, for each available species. However, please note that inconsistency in naming of targets may lead to data for the same target being reported across multiple charts. ✖ |
Peptide Sequence  |
|
|
APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQI MRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGP CSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR |
|
| Selected 3D Structures | ||
|
||
| Post-translational Modification | |
| Homodimer formed by interchain disulphide bonds between cysteine residues at positions 51 and 60; further disulphide bonds formed between cysteine residues at positions 26 and 68, 57 and 102, and 61 and 104. Lysine residues at positions 121, 123 and 126 are N6-acetyllysine. N-linked glycosylation of asparagine residue at position 75 | |
