1xnl
From Proteopedia
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|PDB= 1xnl |SIZE=350|CAPTION= <scene name='initialview01'>1xnl</scene> | |PDB= 1xnl |SIZE=350|CAPTION= <scene name='initialview01'>1xnl</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xnl OCA], [http://www.ebi.ac.uk/pdbsum/1xnl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xnl RCSB]</span> | ||
}} | }} | ||
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[[Category: Kantchev, E A.]] | [[Category: Kantchev, E A.]] | ||
[[Category: Wu, C W.]] | [[Category: Wu, C W.]] | ||
| - | [[Category: NH2]] | ||
[[Category: fusion protein]] | [[Category: fusion protein]] | ||
[[Category: membrane fusion]] | [[Category: membrane fusion]] | ||
[[Category: virus entry]] | [[Category: virus entry]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:07 2008'' |
Revision as of 21:52, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 of sequence from [1]. 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
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