2orz
From Proteopedia
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Structural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin
Overview
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.
About this Structure
2ORZ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis for ligand and heparin binding to neuropilin B domains., Vander Kooi CW, Jusino MA, Perman B, Neau DB, Bellamy HD, Leahy DJ, Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6152-7. Epub 2007 Apr 3. PMID:17405859
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