Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2.

2.50
Hdl Handle:
http://hdl.handle.net/10033/320795
Title:
Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2.
Authors:
Lehtimäki, Mari; Laulumaa, Saara; Ruskamo, Salla; Kursula, Petri ( 0000-0001-8529-3751 )
Abstract:
The myelin sheath is a multilayered membrane that surrounds and insulates axons in the nervous system. One of the proteins specific to the peripheral nerve myelin is P2, a protein that is able to stack lipid bilayers. With the goal of obtaining detailed information on the structure-function relationship of P2, 14 structure-based mutated variants of human P2 were generated and produced. The mutants were designed to potentially affect the binding of lipid bilayers by P2. All mutated variants were also crystallized and preliminary crystallographic data are presented. The structural data from the mutants will be combined with diverse functional assays in order to elucidate the fine details of P2 function at the molecular level.
Citation:
Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2. 2012, 68 (Pt 11):1359-62 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Issue Date:
1-Nov-2012
URI:
http://hdl.handle.net/10033/320795
DOI:
10.1107/S1744309112039036
PubMed ID:
23143249
Type:
Article
Language:
en
ISSN:
1744-3091
Appears in Collections:
publications of the research group CSSB

Full metadata record

DC FieldValue Language
dc.contributor.authorLehtimäki, Marien
dc.contributor.authorLaulumaa, Saaraen
dc.contributor.authorRuskamo, Sallaen
dc.contributor.authorKursula, Petrien
dc.date.accessioned2014-06-11T13:22:33Zen
dc.date.available2014-06-11T13:22:33Zen
dc.date.issued2012-11-01en
dc.identifier.citationProduction and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2. 2012, 68 (Pt 11):1359-62 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.en
dc.identifier.issn1744-3091en
dc.identifier.pmid23143249en
dc.identifier.doi10.1107/S1744309112039036en
dc.identifier.urihttp://hdl.handle.net/10033/320795en
dc.description.abstractThe myelin sheath is a multilayered membrane that surrounds and insulates axons in the nervous system. One of the proteins specific to the peripheral nerve myelin is P2, a protein that is able to stack lipid bilayers. With the goal of obtaining detailed information on the structure-function relationship of P2, 14 structure-based mutated variants of human P2 were generated and produced. The mutants were designed to potentially affect the binding of lipid bilayers by P2. All mutated variants were also crystallized and preliminary crystallographic data are presented. The structural data from the mutants will be combined with diverse functional assays in order to elucidate the fine details of P2 function at the molecular level.en
dc.language.isoenen
dc.rightsArchived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communicationsen
dc.subject.meshAmino Acid Substitutionen
dc.subject.meshCrystallizationen
dc.subject.meshEscherichia colien
dc.subject.meshHumansen
dc.subject.meshHydrophobic and Hydrophilic Interactionsen
dc.subject.meshModels, Molecularen
dc.subject.meshMutagenesis, Site-Directeden
dc.subject.meshMyelin P2 Proteinen
dc.subject.meshProtein Structure, Secondaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshX-Ray Diffractionen
dc.titleProduction and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2.en
dc.typeArticleen
dc.identifier.journalActa crystallographica. Section F, Structural biology and crystallization communicationsen

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