2ORX

Structural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin

2ORX の概要

• エントリーDOI: 10.2210/pdb2orx/pdb
• 分子名称: Neuropilin-1 (2 entities in total)
• 機能のキーワード: neuropilin, vegf, tuftsin, signaling protein, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: Q9QWJ9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35725.52

構造登録者

Vander Kooi, C.W.,Jusino, M.A.,Perman, B.,Neau, D.B.,Bellamy, H.D.,Leahy, D.J. (登録日: 2007-02-05, 公開日: 2007-04-03, 最終更新日: 2024-10-30)

主引用文献

Vander Kooi, C.W.,Jusino, M.A.,Perman, B.,Neau, D.B.,Bellamy, H.D.,Leahy, D.J.
Structural basis for ligand and heparin binding to neuropilin B domains
Proc.Natl.Acad.Sci.Usa, 104:6152-6157, 2007

PubMed Abstract: Neuropilin (Nrp) is a cell surface receptor with essential roles in angiogenesis and axon guidance. Interactions between Nrp and the positively charged C termini of its ligands, VEGF and semaphorin, are mediated by Nrp domains b1 and b2, which share homology to coagulation factor domains. We report here the crystal structure of the tandem b1 and b2 domains of Nrp-1 (N1b1b2) and show that they form a single structural unit. Cocrystallization of N1b1b2 with Tuftsin, a peptide mimic of the VEGF C terminus, reveals the site of interaction with the basic tail of VEGF on the b1 domain. We also show that heparin promotes N1b1b2 dimerization and map the heparin binding site on N1b1b2. These results provide a detailed picture of interactions at the core of the Nrp signaling complex and establish a molecular basis for the synergistic effects of heparin on Nrp-mediated signaling.

PubMed: 17405859
DOI: 10.1073/pnas.0700043104

実験手法

X-RAY DIFFRACTION (2.4 Å)