1fw5
From Proteopedia
(New page: 200px<br /><applet load="1fw5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fw5" /> '''SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTI...) |
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| - | [[Image:1fw5.gif|left|200px]]<br /><applet load="1fw5" size=" | + | [[Image:1fw5.gif|left|200px]]<br /><applet load="1fw5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fw5" /> | caption="1fw5" /> | ||
'''SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS MRNA CAPPING ENZYME NSP1'''<br /> | '''SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS MRNA CAPPING ENZYME NSP1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The RNA replication complex of Semliki Forest virus is bound to | + | The RNA replication complex of Semliki Forest virus is bound to cytoplasmic membranes via the mRNA-capping enzyme Nsp1. Here we have studied the structure and liposome interactions of a synthetic peptide (245)GSTLYTESRKLLRSWHLPSV(264) corresponding to the membrane binding domain of Nsp1. The peptide interacted with liposomes only if negatively charged lipids were present that induced a structural change in the peptide from a random coil to a partially alpha-helical conformation. NMR structure shows that the alpha-helix is amphipathic, the hydrophobic surface consisting of several leucines, a valine, and a tryptophan moiety (Trp-259). Fluorescence studies revealed that this tryptophan intercalates in the bilayer to the depth of the ninth and tenth carbons of lipid acyl chains. Mutation W259A altered the mode of bilayer association of the peptide and abolished its ability to compete for membrane association of intact Nsp1, demonstrating its crucial role in the membrane association and function of Nsp1. |
==About this Structure== | ==About this Structure== | ||
| - | 1FW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1FW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:15 2008'' |
Revision as of 10:43, 21 February 2008
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SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS MRNA CAPPING ENZYME NSP1
Overview
The RNA replication complex of Semliki Forest virus is bound to cytoplasmic membranes via the mRNA-capping enzyme Nsp1. Here we have studied the structure and liposome interactions of a synthetic peptide (245)GSTLYTESRKLLRSWHLPSV(264) corresponding to the membrane binding domain of Nsp1. The peptide interacted with liposomes only if negatively charged lipids were present that induced a structural change in the peptide from a random coil to a partially alpha-helical conformation. NMR structure shows that the alpha-helix is amphipathic, the hydrophobic surface consisting of several leucines, a valine, and a tryptophan moiety (Trp-259). Fluorescence studies revealed that this tryptophan intercalates in the bilayer to the depth of the ninth and tenth carbons of lipid acyl chains. Mutation W259A altered the mode of bilayer association of the peptide and abolished its ability to compete for membrane association of intact Nsp1, demonstrating its crucial role in the membrane association and function of Nsp1.
About this Structure
1FW5 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Membrane binding mechanism of an RNA virus-capping enzyme., Lampio A, Kilpelainen I, Pesonen S, Karhi K, Auvinen P, Somerharju P, Kaariainen L, J Biol Chem. 2000 Dec 1;275(48):37853-9. PMID:10984480
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