1lg7

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(New page: 200px<br /><applet load="1lg7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lg7, resolution 1.96&Aring;" /> '''Crystal structure of...)
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caption="1lg7, resolution 1.96&Aring;" />
caption="1lg7, resolution 1.96&Aring;" />
'''Crystal structure of Vesicular Stomatitis Virus Matrix Protein'''<br />
'''Crystal structure of Vesicular Stomatitis Virus Matrix Protein'''<br />
==Overview==
==Overview==
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The vesicular stomatitis virus (VSV) matrix protein (M) interacts with, cellular membranes, self-associates and plays a major role in virus, assembly and budding. We present the crystallographic structure, determined at 1.96 A resolution, of a soluble thermolysin resistant core, of VSV M. The fold is a new fold shared by the other vesiculovirus matrix, proteins. The structure accounts for the loss of stability of M, temperature-sensitive mutants deficient in budding, and reveals a flexible, loop protruding from the globular core that is important for, self-assembly. Membrane floatation shows that, together with the M, lysine-rich N-terminal peptide, a second domain of the protein is involved, in membrane binding. Indeed, the structure reveals a hydrophobic surface, located close to the hydrophobic loop and surrounded by conserved basic, residues that may constitute this domain. Lastly, comparison of the, negative-stranded virus matrix proteins with retrovirus Gag proteins, suggests that the flexible link between their major membrane binding, domain and the rest of the structure is a common feature shared by these, proteins involved in budding and virus assembly.
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The vesicular stomatitis virus (VSV) matrix protein (M) interacts with cellular membranes, self-associates and plays a major role in virus assembly and budding. We present the crystallographic structure, determined at 1.96 A resolution, of a soluble thermolysin resistant core of VSV M. The fold is a new fold shared by the other vesiculovirus matrix proteins. The structure accounts for the loss of stability of M temperature-sensitive mutants deficient in budding, and reveals a flexible loop protruding from the globular core that is important for self-assembly. Membrane floatation shows that, together with the M lysine-rich N-terminal peptide, a second domain of the protein is involved in membrane binding. Indeed, the structure reveals a hydrophobic surface located close to the hydrophobic loop and surrounded by conserved basic residues that may constitute this domain. Lastly, comparison of the negative-stranded virus matrix proteins with retrovirus Gag proteins suggests that the flexible link between their major membrane binding domain and the rest of the structure is a common feature shared by these proteins involved in budding and virus assembly.
==About this Structure==
==About this Structure==
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1LG7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vesicular_stomatitis_virus Vesicular stomatitis virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LG7 OCA].
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1LG7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vesicular_stomatitis_virus Vesicular stomatitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LG7 OCA].
==Reference==
==Reference==
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[[Category: virus matrix]]
[[Category: virus matrix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:32:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:44 2008''

Revision as of 11:44, 21 February 2008


1lg7, resolution 1.96Å

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Crystal structure of Vesicular Stomatitis Virus Matrix Protein

Overview

The vesicular stomatitis virus (VSV) matrix protein (M) interacts with cellular membranes, self-associates and plays a major role in virus assembly and budding. We present the crystallographic structure, determined at 1.96 A resolution, of a soluble thermolysin resistant core of VSV M. The fold is a new fold shared by the other vesiculovirus matrix proteins. The structure accounts for the loss of stability of M temperature-sensitive mutants deficient in budding, and reveals a flexible loop protruding from the globular core that is important for self-assembly. Membrane floatation shows that, together with the M lysine-rich N-terminal peptide, a second domain of the protein is involved in membrane binding. Indeed, the structure reveals a hydrophobic surface located close to the hydrophobic loop and surrounded by conserved basic residues that may constitute this domain. Lastly, comparison of the negative-stranded virus matrix proteins with retrovirus Gag proteins suggests that the flexible link between their major membrane binding domain and the rest of the structure is a common feature shared by these proteins involved in budding and virus assembly.

About this Structure

1LG7 is a Single protein structure of sequence from Vesicular stomatitis virus. Full crystallographic information is available from OCA.

Reference

Crystal structure of vesicular stomatitis virus matrix protein., Gaudier M, Gaudin Y, Knossow M, EMBO J. 2002 Jun 17;21(12):2886-92. PMID:12065402

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