2pdz: Difference between revisions

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[[Image:2pdz.jpg|left|200px]]<br /><applet load="2pdz" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2pdz.jpg|left|200px]]<br /><applet load="2pdz" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2pdz" />

'''SOLUTION STRUCTURE OF THE SYNTROPHIN PDZ DOMAIN IN COMPLEX WITH THE PEPTIDE GVKESLV, NMR, 15 STRUCTURES'''<br />

==Overview==

Syntrophins are modular proteins belonging to the dystrophin associated, glycoprotein complex and are thought to be involved in the regulation of, the muscular system. Screening of peptide libraries revealed selectivity, of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO- found, to be highly conserved in the alpha-subunit C-terminus of vertebrate, voltage gated sodium channels (VGSCs). The solution structure of the, domain in complex with the peptide G-V-K-E-S-L-V shows specific, interactions between the conserved residues in the peptide and, syntrophin-characteristic residues in the domain. We propose that, syntrophins localize VGSCs to the dystrophin network through its PDZ, domain.

Syntrophins are modular proteins belonging to the dystrophin associated glycoprotein complex and are thought to be involved in the regulation of the muscular system. Screening of peptide libraries revealed selectivity of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO- found to be highly conserved in the alpha-subunit C-terminus of vertebrate voltage gated sodium channels (VGSCs). The solution structure of the domain in complex with the peptide G-V-K-E-S-L-V shows specific interactions between the conserved residues in the peptide and syntrophin-characteristic residues in the domain. We propose that syntrophins localize VGSCs to the dystrophin network through its PDZ domain.

==About this Structure==

2PDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2PDZ OCA].

2PDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDZ OCA].

==Reference==

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[[Category: voltage-gated sodium channel]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 13:30:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:27 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2pdz.jpg|left|200px]]<br /><applet load="2pdz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2pdz.jpg|left|200px]]<br /><applet load="2pdz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2pdz" />
 '''SOLUTION STRUCTURE OF THE SYNTROPHIN PDZ DOMAIN IN COMPLEX WITH THE PEPTIDE GVKESLV, NMR, 15 STRUCTURES'''<br />
 ==Overview==
-Syntrophins are modular proteins belonging to the dystrophin associated, glycoprotein complex and are thought to be involved in the regulation of, the muscular system. Screening of peptide libraries revealed selectivity, of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO- found, to be highly conserved in the alpha-subunit C-terminus of vertebrate, voltage gated sodium channels (VGSCs). The solution structure of the, domain in complex with the peptide G-V-K-E-S-L-V shows specific, interactions between the conserved residues in the peptide and, syntrophin-characteristic residues in the domain. We propose that, syntrophins localize VGSCs to the dystrophin network through its PDZ, domain.
+Syntrophins are modular proteins belonging to the dystrophin associated glycoprotein complex and are thought to be involved in the regulation of the muscular system. Screening of peptide libraries revealed selectivity of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO- found to be highly conserved in the alpha-subunit C-terminus of vertebrate voltage gated sodium channels (VGSCs). The solution structure of the domain in complex with the peptide G-V-K-E-S-L-V shows specific interactions between the conserved residues in the peptide and syntrophin-characteristic residues in the domain. We propose that syntrophins localize VGSCs to the dystrophin network through its PDZ domain.
 ==About this Structure==
-PDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PDZ OCA].
+PDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDZ OCA].
 ==Reference==
@@ Line 26: / Line 26: @@
 [[Category: voltage-gated sodium channel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:30:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:27 2008''