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dc.contributor.authorWang, Conan K
dc.contributor.authorSimon, Anne
dc.contributor.authorJessen, Christian M
dc.contributor.authorOliveira, Cristiano LP
dc.contributor.authorMack, Lynsey
dc.contributor.authorBraunewell, Karl-Heinz
dc.contributor.authorAmes, James B
dc.contributor.authorPedersen, Jan Skov
dc.contributor.authorHofmann, Andreas
dc.date.accessioned2017-05-03T15:19:01Z
dc.date.available2017-05-03T15:19:01Z
dc.date.issued2011
dc.date.modified2012-02-13T05:07:53Z
dc.identifier.issn1932-6203
dc.identifier.doi10.1371/journal.pone.0026793
dc.identifier.urihttp://hdl.handle.net/10072/42481
dc.description.abstractThe 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.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent640945 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherPublic Library of Science
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrome26793-1
dc.relation.ispartofpagetoe26793-10
dc.relation.ispartofissue11
dc.relation.ispartofjournalPloS One
dc.relation.ispartofvolume6
dc.rights.retentionN
dc.subject.fieldofresearchStructural biology (incl. macromolecular modelling)
dc.subject.fieldofresearchcode310112
dc.titleDivalent Cations and Redox Conditions Regulate the Molecular Structure and Function of Visinin-Like Protein-1
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://www.plos.org/journals/license.html
gro.facultyGriffith 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.issued2011
gro.hasfulltextFull Text
gro.griffith.authorHofmann, Andreas
gro.griffith.authorWang, Conan K.


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