dc.contributor.author | Wang, Conan K | |
dc.contributor.author | Simon, Anne | |
dc.contributor.author | Jessen, Christian M | |
dc.contributor.author | Oliveira, Cristiano LP | |
dc.contributor.author | Mack, Lynsey | |
dc.contributor.author | Braunewell, Karl-Heinz | |
dc.contributor.author | Ames, James B | |
dc.contributor.author | Pedersen, Jan Skov | |
dc.contributor.author | Hofmann, Andreas | |
dc.date.accessioned | 2017-05-03T15:19:01Z | |
dc.date.available | 2017-05-03T15:19:01Z | |
dc.date.issued | 2011 | |
dc.date.modified | 2012-02-13T05:07:53Z | |
dc.identifier.issn | 1932-6203 | |
dc.identifier.doi | 10.1371/journal.pone.0026793 | |
dc.identifier.uri | http://hdl.handle.net/10072/42481 | |
dc.description.abstract | The NCS protein Visinin-like Protein 1 (VILIP-1) transduces calcium signals in the brain and serves as an effector of the non-retinal receptor guanylyl cyclases (GCs) GC-A and GC-B, and nicotinic acetyl choline receptors (nAchR). Analysis of the quaternary structure of VILIP-1 in solution reveals the existence of monomeric and dimeric species, the relative contents of which are affected but not exclusively regulated by divalent metal ions and Redox conditions. Using small-angle X-ray scattering, we have investigated the low resolution structure of the calcium-bound VILIP-1 dimer under reducing conditions. Scattering profiles for samples with high monomeric and dimeric contents have been obtained. The dimerization interface involves residues from EF-hand regions EF3 and EF4. Using monolayer adsorption experiments, we show that myristoylated and unmyristoylated VILIP-1 can bind lipid membranes. The presence of calcium only marginally improves binding of the protein to the monolayer, suggesting that charged residues at the protein surface may play a role in the binding process. In the presence of calcium, VILIP-1 undergoes a conformational re-arrangement, exposing previously hidden surfaces for interaction with protein partners. We hypothesise a working model where dimeric VILIP-1 interacts with the membrane where it binds membrane-bound receptors in a calcium-dependent manner. | |
dc.description.peerreviewed | Yes | |
dc.description.publicationstatus | Yes | |
dc.format.extent | 640945 bytes | |
dc.format.mimetype | application/pdf | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Public Library of Science | |
dc.publisher.place | United States | |
dc.relation.ispartofstudentpublication | N | |
dc.relation.ispartofpagefrom | e26793-1 | |
dc.relation.ispartofpageto | e26793-10 | |
dc.relation.ispartofissue | 11 | |
dc.relation.ispartofjournal | PloS One | |
dc.relation.ispartofvolume | 6 | |
dc.rights.retention | N | |
dc.subject.fieldofresearch | Structural biology (incl. macromolecular modelling) | |
dc.subject.fieldofresearchcode | 310112 | |
dc.title | Divalent Cations and Redox Conditions Regulate the Molecular Structure and Function of Visinin-Like Protein-1 | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
dcterms.license | http://www.plos.org/journals/license.html | |
gro.faculty | Griffith Sciences, Griffith Institute for Drug Discovery | |
gro.rights.copyright | © 2011, Wang et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License CCAL. (http://www.plos.org/journals/license.html) | |
gro.date.issued | 2011 | |
gro.hasfulltext | Full Text | |
gro.griffith.author | Hofmann, Andreas | |
gro.griffith.author | Wang, Conan K. | |