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2rlj

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{{STRUCTURE_2rlj| PDB=2rlj | SCENE= }}
{{STRUCTURE_2rlj| PDB=2rlj | SCENE= }}
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'''NMR Structure of Ebola fusion peptide in SDS micelles at pH 7'''
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===NMR Structure of Ebola fusion peptide in SDS micelles at pH 7===
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==Overview==
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The fusion peptide EBO(16) (GAAIGLAWIPYFGPAA) comprises the fusion domain of an internal sequence located in the envelope fusion glycoprotein (GP2) of the Ebola virus. This region interacts with the cellular membrane of the host and leads to membrane fusion. To gain insight into the mechanism of the peptide-membrane interaction and fusion, insertion of the peptide was modeled by experiments in which the tryptophan fluorescence and (1)H NMR were monitored in the presence of sodium dodecyl sulfate micelles or in the presence of detergent-resistant membrane fractions. In the presence of SDS micelles, EBO(16) undergoes a random coil-helix transition, showing a tendency to self-associate. The three-dimensional structure displays a 3(10)-helix in the central part of molecule, similar to the fusion peptides of many known membrane fusion proteins. Our results also reveal that EBO(16) can interact with detergent-resistant membrane fractions and strongly suggest that Trp-8 and Phe-12 are important for structure maintenance within the membrane bilayer. Replacement of tryptophan 8 with alanine (W8A) resulted in dramatic loss of helical structure, proving the importance of the aromatic ring in stabilizing the helix. Molecular dynamics studies of the interaction between the peptide and the target membrane also corroborated the crucial participation of these aromatic residues. The aromatic-aromatic interaction may provide a mechanism for the free energy coupling between random coil-helical transition and membrane anchoring. Our data shed light on the structural "domains" of fusion peptides and provide a clue for the development of a drug that might block the early steps of viral infection.
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(as it appears on PubMed at http://www.pubmed.gov), where 17545161 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17545161}}
==About this Structure==
==About this Structure==
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2RLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zaire_ebolavirus Zaire ebolavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLJ OCA].
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2RLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zaire_ebolavirus Zaire ebolavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLJ OCA].
==Reference==
==Reference==
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[[Category: Solution nmr]]
[[Category: Solution nmr]]
[[Category: Viral protein]]
[[Category: Viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:08:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:06:16 2008''

Revision as of 01:06, 28 July 2008

Image:2rlj.png

Template:STRUCTURE 2rlj

NMR Structure of Ebola fusion peptide in SDS micelles at pH 7

Template:ABSTRACT PUBMED 17545161

About this Structure

2RLJ is a Single protein structure of sequence from Zaire ebolavirus. Full experimental information is available from OCA.

Reference

Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts., Freitas MS, Gaspar LP, Lorenzoni M, Almeida FC, Tinoco LW, Almeida MS, Maia LF, Degreve L, Valente AP, Silva JL, J Biol Chem. 2007 Sep 14;282(37):27306-14. Epub 2007 Jun 1. PMID:17545161

Page seeded by OCA on Mon Jul 28 04:06:16 2008

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