1pd3: Difference between revisions

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[[Image:1pd3.gif|left|200px]]<br /><applet load="1pd3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pd3.gif|left|200px]]<br /><applet load="1pd3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pd3, resolution 2.60Å" />

'''Influenza A NEP M1-binding domain'''<br />

==Overview==

During influenza virus infection, viral ribonucleoproteins (vRNPs) are, replicated in the nucleus and must be exported to the cytoplasm before, assembling into mature viral particles. Nuclear export is mediated by the, cellular protein Crm1 and putatively by the viral protein NEP/NS2., Proteolytic cleavage of NEP defines an N-terminal domain which mediates, RanGTP-dependent binding to Crm1 and a C-terminal domain which binds to, the viral matrix protein M1. The 2.6 A crystal structure of the C-terminal, domain reveals an amphipathic helical hairpin which dimerizes as a, four-helix bundle. The NEP-M1 interaction involves two critical epitopes:, an exposed tryptophan (Trp78) surrounded by a cluster of glutamate, residues on NEP, and the basic nuclear localization signal (NLS) of M1., Implications for vRNP export are discussed.

During influenza virus infection, viral ribonucleoproteins (vRNPs) are replicated in the nucleus and must be exported to the cytoplasm before assembling into mature viral particles. Nuclear export is mediated by the cellular protein Crm1 and putatively by the viral protein NEP/NS2. Proteolytic cleavage of NEP defines an N-terminal domain which mediates RanGTP-dependent binding to Crm1 and a C-terminal domain which binds to the viral matrix protein M1. The 2.6 A crystal structure of the C-terminal domain reveals an amphipathic helical hairpin which dimerizes as a four-helix bundle. The NEP-M1 interaction involves two critical epitopes: an exposed tryptophan (Trp78) surrounded by a cluster of glutamate residues on NEP, and the basic nuclear localization signal (NLS) of M1. Implications for vRNP export are discussed.

==About this Structure==

1PD3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PD3 OCA].

1PD3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PD3 OCA].

==Reference==

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[[Category: nep/ns2]]

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@@ Line 1: / Line 1: @@
-[[Image:1pd3.gif|left|200px]]<br /><applet load="1pd3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pd3.gif|left|200px]]<br /><applet load="1pd3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pd3, resolution 2.60&Aring;" />
 '''Influenza A NEP M1-binding domain'''<br />
 ==Overview==
-During influenza virus infection, viral ribonucleoproteins (vRNPs) are, replicated in the nucleus and must be exported to the cytoplasm before, assembling into mature viral particles. Nuclear export is mediated by the, cellular protein Crm1 and putatively by the viral protein NEP/NS2., Proteolytic cleavage of NEP defines an N-terminal domain which mediates, RanGTP-dependent binding to Crm1 and a C-terminal domain which binds to, the viral matrix protein M1. The 2.6 A crystal structure of the C-terminal, domain reveals an amphipathic helical hairpin which dimerizes as a, four-helix bundle. The NEP-M1 interaction involves two critical epitopes:, an exposed tryptophan (Trp78) surrounded by a cluster of glutamate, residues on NEP, and the basic nuclear localization signal (NLS) of M1., Implications for vRNP export are discussed.
+During influenza virus infection, viral ribonucleoproteins (vRNPs) are replicated in the nucleus and must be exported to the cytoplasm before assembling into mature viral particles. Nuclear export is mediated by the cellular protein Crm1 and putatively by the viral protein NEP/NS2. Proteolytic cleavage of NEP defines an N-terminal domain which mediates RanGTP-dependent binding to Crm1 and a C-terminal domain which binds to the viral matrix protein M1. The 2.6 A crystal structure of the C-terminal domain reveals an amphipathic helical hairpin which dimerizes as a four-helix bundle. The NEP-M1 interaction involves two critical epitopes: an exposed tryptophan (Trp78) surrounded by a cluster of glutamate residues on NEP, and the basic nuclear localization signal (NLS) of M1. Implications for vRNP export are discussed.
 ==About this Structure==
-PD3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PD3 OCA].
+PD3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PD3 OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: nep/ns2]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:42:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:35 2008''