Ontology highlight
ABSTRACT:
SUBMITTER: Vander Kooi CW
PROVIDER: S-EPMC1851056 | biostudies-literature | 2007 Apr
REPOSITORIES: biostudies-literature
Vander Kooi Craig W CW Jusino Manuel A MA Perman Benjamin B Neau David B DB Bellamy Henry D HD Leahy Daniel J DJ
Proceedings of the National Academy of Sciences of the United States of America 20070403 15
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 t ...[more]