1VGH

HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR, 20 STRUCTURES

1VGH の概要

• エントリーDOI: 10.2210/pdb1vgh/pdb
• NMR情報: BMRB: 5238
• 分子名称: VASCULAR ENDOTHELIAL GROWTH FACTOR-165 (1 entity in total)
• 機能のキーワード: heparin-binding, angiogenesis, growth factor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P15692
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6496.48

構造登録者

Fairbrother, W.J.,Champe, M.A.,Christinger, H.W.,Keyt, B.A.,Starovasnik, M.A. (登録日: 1997-12-17, 公開日: 1998-04-08, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

SOLUTION NMR