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Article

Molecular mapping and functional characterization of the VEGF164 heparin-binding domain.

The Journal of biological chemistry - 21 Sept 2007

Krilleke Dominik, DeErkenez Andrea, Schubert William, Giri Indrajit, Robinson Gregory S, Ng Yin-Shan, Shima David T

Abstract excerpt

The longer splice isoforms of vascular endothelial growth factor-A (VEGF-A), including mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the ability of these isoforms to be deposited in the heparan sulfate-rich extracellular matrix and to interact with the prototype sulfated glycosaminoglycan, heparin. The shortest isoform, VEGF120, lacks this highly basic domain and is freely...

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Topics

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Share to Endothelial Cells
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Protein Structure, Secondary

Share to Protein Structure, Tertiary

Share to Sequence Homology, Amino Acid

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Source

Identifiers

PMID: 17626017
DOI: 10.1074/jbc.M700319200

Genes

HBD
NRP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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