We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1xnl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xnl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xnl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xnl| PDB=1xnl | SCENE= }}
{{STRUCTURE_1xnl| PDB=1xnl | SCENE= }}
-
'''ASLV fusion peptide'''
+
===ASLV fusion peptide===
-
==Overview==
+
<!--
-
The structure and membrane interaction of the internal fusion peptide (IFP) fragment of the avian sarcoma and leucosis virus (ASLV) envelope glycoprotein was studied by an array of biophysical methods. The peptide was found to induce lipid mixing of vesicles more strongly than the fusion peptide derived from the N-terminal fusion peptide of influenza virus (HA2-FP). It was observed that the helical structure was enhanced in association with the model membranes, particularly in the N-terminal portion of the peptide. According to the infrared study, the peptide inserted into the membrane in an oblique orientation, but less deeply than the influenza HA2-FP. Analysis of NMR data in sodium dodecyl sulfate micelle suspension revealed that Pro13 of the peptide was located near the micelle-water interface. A type II beta-turn was deduced from NMR data for the peptide in aqueous medium, demonstrating a conformational flexibility of the IFP in analogy to the N-terminal FP such as that of gp41. A loose and multimodal self-assembly was deduced from the rhodamine fluorescence self-quenching experiments for the peptide bound to the membrane bilayer. Oligomerization of the peptide and its variants can also be observed in the electrophoretic experiments, suggesting a property in common with other N-terminal FP of class I fusion proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15606759}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15606759 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15606759}}
==About this Structure==
==About this Structure==
-
1XNL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNL OCA].
+
1XNL is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNL OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Membrane fusion]]
[[Category: Membrane fusion]]
[[Category: Virus entry]]
[[Category: Virus entry]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:16:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:17:51 2008''

Revision as of 03:17, 28 July 2008

Image:1xnl.png

Template:STRUCTURE 1xnl

ASLV fusion peptide

Template:ABSTRACT PUBMED 15606759

About this Structure

1XNL is a Single protein structure. Full experimental information is available from OCA.

Reference

Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus., Cheng SF, Wu CW, Kantchev EA, Chang DK, Eur J Biochem. 2004 Dec;271(23-24):4725-36. PMID:15606759

Page seeded by OCA on Mon Jul 28 06:17:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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