2orx
From Proteopedia
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'''Structural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin''' | '''Structural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin''' | ||
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| + | ==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== | ==About this Structure== | ||
2ORX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORX OCA]. | 2ORX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORX OCA]. | ||
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| + | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17405859 17405859] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Neau, D B.]] | [[Category: Neau, D B.]] | ||
[[Category: Perman, B.]] | [[Category: Perman, B.]] | ||
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | [[Category: | + | [[Category: Neuropilin]] |
| - | [[Category: | + | [[Category: Signaling protein]] |
| - | + | [[Category: Tuftsin]] | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | [[Category: Vegf]] |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:30:04 2008'' | ||
Revision as of 10:30, 30 April 2008
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
2ORX 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 Page seeded by OCA on Wed Apr 30 13:30:04 2008
