1XNL
ASLV fusion peptide
Summary for 1XNL
| Entry DOI | 10.2210/pdb1xnl/pdb |
| Descriptor | membrane protein gp37 (1 entity in total) |
| Functional Keywords | fusion protein, virus entry, membrane fusion, viral protein |
| Cellular location | Transmembrane protein: Virion membrane; Single-pass type I membrane protein (By similarity). Surface protein: Virion membrane; Peripheral membrane protein: P03397 |
| Total number of polymer chains | 1 |
| Total formula weight | 2864.35 |
| Authors | Cheng, S.F.,Wu, C.W.,Kantchev, E.A.,Chang, D.K. (deposition date: 2004-10-05, release date: 2005-01-11, Last modification date: 2024-10-16) |
| Primary citation | Cheng, S.F.,Wu, C.W.,Kantchev, E.A.,Chang, D.K. Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus Eur.J.Biochem., 271:4725-4736, 2004 Cited by PubMed Abstract: 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. PubMed: 15606759DOI: 10.1111/j.1432-1033.2004.04436.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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