2VGH

HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 2VGH

• Entry DOI: 10.2210/pdb2vgh/pdb
• NMR Information: BMRB: 5238
• Descriptor: VASCULAR ENDOTHELIAL GROWTH FACTOR-165 (1 entity in total)
• Functional Keywords: growth factor, heparin-binding, angiogenesis
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P15692
• Total number of polymer chains: 1
• Total formula weight: 6496.48

Authors

Fairbrother, W.J.,Champe, M.A.,Christinger, H.W.,Keyt, B.A.,Starovasnik, M.A. (deposition date: 1997-12-17, release date: 1998-04-08, Last modification date: 2024-11-20)

Primary citation

Fairbrother, W.J.,Champe, M.A.,Christinger, H.W.,Keyt, B.A.,Starovasnik, M.A.
Solution structure of the heparin-binding domain of vascular endothelial growth factor.
Structure, 6:637-648, 1998

PubMed Abstract: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific mitogen and is a potent angiogenic and vascular permeabilizing factor. VEGF is also an important mediator of pathological angiogenesis associated with cancer, rheumatoid arthritis and proliferative retinopathy. The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate. Heparin binding to VEGF165, the most abundantly expressed isoform of VEGF, has been localized to the carboxy-terminal 55 residues; plasmin cleavage of VEGF165 yields a homodimeric 110-residue amino-terminal receptor-binding domain (VEGF110) and two 55-residue carboxy-terminal heparin-binding fragments. The endothelial cell mitogenic potency of VEGF110 is decreased significantly relative to VEGF165, indicating that the heparin-binding domains are critical for stimulating endothelial cell proliferation.

PubMed: 9634701
DOI: 10.1016/S0969-2126(98)00065-3

Experimental method

SOLUTION NMR