This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fw5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fw5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fw5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fw5| PDB=1fw5 | SCENE= }}
{{STRUCTURE_1fw5| PDB=1fw5 | SCENE= }}
-
'''SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS MRNA CAPPING ENZYME NSP1'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10984480}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10984480 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10984480}}
==About this Structure==
==About this Structure==
-
1FW5 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW5 OCA].
+
1FW5 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW5 OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Somerharju, P.]]
[[Category: Somerharju, P.]]
[[Category: Viral protein]]
[[Category: Viral protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:50:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:02:04 2008''

Revision as of 01:02, 1 July 2008

Image:1fw5.png

Template:STRUCTURE 1fw5

SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS MRNA CAPPING ENZYME NSP1

Template:ABSTRACT PUBMED 10984480

About this Structure

1FW5 is a Single protein structure. Full experimental 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

Page seeded by OCA on Tue Jul 1 04:02:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fw5"
Personal tools