2ala

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{{STRUCTURE_2ala| PDB=2ala | SCENE= }}
{{STRUCTURE_2ala| PDB=2ala | SCENE= }}
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'''Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.'''
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===Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.===
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==Overview==
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Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for inducing membrane fusion, triggered by exposure to the acidic environment of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to interact with the target membrane, and, at the same time, to rearrange into E1 homotrimers that drive the membrane fusion reaction. We previously reported a preliminary Calpha trace of the monomeric E1 glycoprotein ectodomain and its organization on the virus particle. We also reported the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution and describe the amino acids involved in contacts in the virion. These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly.
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The line below this paragraph, {{ABSTRACT_PUBMED_16407067}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16407067 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16407067}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus., Roussel A, Lescar J, Vaney MC, Wengler G, Wengler G, Rey FA, Structure. 2006 Jan;14(1):75-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16407067 16407067]
Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus., Roussel A, Lescar J, Vaney MC, Wengler G, Wengler G, Rey FA, Structure. 2006 Jan;14(1):75-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16407067 16407067]
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The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH., Lescar J, Roussel A, Wien MW, Navaza J, Fuller SD, Wengler G, Wengler G, Rey FA, Cell. 2001 Apr 6;105(1):137-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11301009 11301009]
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Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus., Gibbons DL, Vaney MC, Roussel A, Vigouroux A, Reilly B, Lepault J, Kielian M, Rey FA, Nature. 2004 Jan 22;427(6972):320-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14737160 14737160]
[[Category: Semliki forest virus]]
[[Category: Semliki forest virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Membrane fusion]]
[[Category: Membrane fusion]]
[[Category: Viral protein]]
[[Category: Viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:11:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:50:02 2008''

Revision as of 00:50, 28 July 2008

Image:2ala.png

Template:STRUCTURE 2ala

Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.

Template:ABSTRACT PUBMED 16407067

About this Structure

2ALA is a Single protein structure of sequence from Semliki forest virus. Full crystallographic information is available from OCA.

Reference

Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus., Roussel A, Lescar J, Vaney MC, Wengler G, Wengler G, Rey FA, Structure. 2006 Jan;14(1):75-86. PMID:16407067

The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH., Lescar J, Roussel A, Wien MW, Navaza J, Fuller SD, Wengler G, Wengler G, Rey FA, Cell. 2001 Apr 6;105(1):137-48. PMID:11301009

Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus., Gibbons DL, Vaney MC, Roussel A, Vigouroux A, Reilly B, Lepault J, Kielian M, Rey FA, Nature. 2004 Jan 22;427(6972):320-5. PMID:14737160

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