1xnl
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1xnl.gif|left|200px]] | [[Image:1xnl.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1xnl", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1xnl| PDB=1xnl | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ASLV fusion peptide''' | '''ASLV fusion peptide''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1XNL is a [[Single protein]] structure | + | 1XNL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNL OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 25: | ||
[[Category: Kantchev, E A.]] | [[Category: Kantchev, E A.]] | ||
[[Category: Wu, C W.]] | [[Category: Wu, C W.]] | ||
| - | [[Category: | + | [[Category: Fusion protein]] |
| - | [[Category: | + | [[Category: Membrane fusion]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 12:16, 3 May 2008
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.
About this Structure
1XNL is a Single protein structure. Full crystallographic 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 Sat May 3 15:16:06 2008
