Group:MUZIC:ALP: Difference between revisions

Line 32:

==Function and Interactions==

All member proteins of ALP subfamily have been shown to interact with component proteins of the cytoskeleton, particularly α-actinin. Interestingly, a non-structural interacting partner as recently been identified <ref name="e">doi:10.1371/journal.pone.0019511</ref>~~, where the PDZ domain of mystique (human PDLIM2) selectively interacts with the highly pathogenic bird flu virus (NS1) C-terminal peptide~~. An elegant summary of ~~many~~ other molecular interactions and plausible functions of member proteins of ALP subfamily is presented by Zheng M ''et al'' (2010) <ref name="c">doi:10.1093/jmcb/mjp038</ref> and te Velthius A.J. ''et al'' (2007) <ref name="d">DOI 10.1100/tsw.2007.232</ref>.

All member proteins of ALP subfamily have been shown to interact with component proteins of the cytoskeleton, particularly α-actinin. Interestingly, a non-structural interacting partner as recently been identified; the PDZ domain of mystique (human PDLIM2) selectively interacts with the highly pathogenic bird flu virus (NS1) peptide<ref name="e">doi:10.1371/journal.pone.0019511</ref>. An elegant summary of other molecular interactions and plausible functions of member proteins of ALP subfamily is presented by Zheng M ''et al'' (2010) <ref name="c">doi:10.1093/jmcb/mjp038</ref> and te Velthius A.J. ''et al'' (2007) <ref name="d">DOI 10.1100/tsw.2007.232</ref>.

Line 44:

==Pathology==

Deficiency in cardiac development and cardiac malfunction resulting from mutation and genetic studies have been identified within the ALP subfamily<ref name="d">DOI 10.1100/tsw.2007.232</ref>, <ref name="c">doi:10.1093/jmcb/mjp038</ref>. Human PDLIM2 (mystique) selectively interacts with highly pathogenic bird flu virus strain H5N1 via its PDZ domain, and as PDLIM2 is localised to the human cardiac muscle, this interaction speculatively tethers the pathogenic viral protein to the heart thereby mediating cardiac dysfunction likely with lethal effects associated to the ~~pathogenic~~ bird flu virus.

Deficiency in cardiac development and cardiac malfunction resulting from mutation and genetic studies have been identified within the ALP subfamily<ref name="d">DOI 10.1100/tsw.2007.232</ref>, <ref name="c">doi:10.1093/jmcb/mjp038</ref>. Human PDLIM2 (mystique) selectively interacts with highly pathogenic bird flu virus strain H5N1 via its PDZ domain, and as PDLIM2 is localised to the human cardiac muscle, this interaction speculatively tethers the pathogenic viral protein to the heart thereby mediating cardiac dysfunction likely with lethal effects associated to the bird flu virus.

Group:MUZIC:ALP: Difference between revisions

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@@ Line 32: / Line 32: @@
 <Structure load='2PKT' size='150' frame='true' align='right' caption='X-ray crystal structure of the PDZ domain of human hCLIM1 in complex with the C-terminal peptide of α-actinin-1 (PDB code: 2PKT)[http://www.pdb.org/pdb/explore/explore.do?structureId=2PKT]'/>
 <Structure load='3PDV' size='150' frame='true' align='right' caption='X-ray crystal structure of the PDZ domain of human PDLIM2 in complex with pathogenic bird flu viral peptide NS1 (PDB code: 3PDV)[http://www.pdb.org/pdb/explore/explore.do?structureId=3PDV]'/>
-<Structure load='1X64' size='150' frame='true' align='right' caption='NMR solution structure of the LIM domain of mouse PDLIM3(ALP)(PDB code: 1X64)[http://www.pdb.org/pdb/explore/explore.do?structureId=1X64]'/>
+<Structure load='1X64' size='150' frame='true' align='right' caption='NMR solution structure of the LIM domain of mouse PDLIM3 (ALP) (PDB code: 1X64)[http://www.pdb.org/pdb/explore/explore.do?structureId=1X64]'/>
-<Structure load='1v51' size='150' frame='true' align='right' caption='NMR solution structure of the PDZ domain of mouse PDLIM3(ALP)(PDB code: 1v51)[http://www.rcsb.org/pdb/explore/explore.do?pdbId=1v5l]'/>
+<Structure load='1v51' size='150' frame='true' align='right' caption='NMR solution structure of the PDZ domain of mouse PDLIM3 (ALP) (PDB code: 1v51)[http://www.rcsb.org/pdb/explore/explore.do?pdbId=1v5l]'/>
-<Structure load='2V1W' size='150' frame='true' align='right' caption='X-ray crystal stucture of the PDZ domain of human PDLIM4 (RIL) in complex with human α-actinin-1(PDB code: 2V1W)[http://www.rcsb.org/pdb/explore/explore.do?structureId=2V1W]'/>
+<Structure load='2V1W' size='150' frame='true' align='right' caption='X-ray crystal stucture of the PDZ domain of human PDLIM4 (RIL) in complex with human α-actinin-1C-terminal peptide (PDB code: 2V1W)[http://www.rcsb.org/pdb/explore/explore.do?structureId=2V1W]'/>
 ==Function and Interactions==
-All member proteins of ALP subfamily have been shown to interact with component proteins of the cytoskeleton, particularly α-actinin. Interestingly, a non-structural interacting partner as recently been identified <ref name="e">doi:10.1371/journal.pone.0019511</ref>, where the PDZ domain of mystique (human PDLIM2) selectively interacts with the highly pathogenic bird flu virus (NS1) C-terminal peptide.  An elegant summary of many other molecular interactions and plausible functions of member proteins of ALP subfamily is presented by Zheng M ''et al'' (2010) <ref name="c">doi:10.1093/jmcb/mjp038</ref> and te Velthius A.J. ''et al'' (2007) <ref name="d">DOI 10.1100/tsw.2007.232</ref>.
+All member proteins of ALP subfamily have been shown to interact with component proteins of the cytoskeleton, particularly α-actinin. Interestingly, a non-structural interacting partner as recently been identified; the PDZ domain of mystique (human PDLIM2) selectively interacts with the highly pathogenic bird flu virus (NS1) peptide<ref name="e">doi:10.1371/journal.pone.0019511</ref>.  An elegant summary of other molecular interactions and plausible functions of member proteins of ALP subfamily is presented by Zheng M ''et al'' (2010) <ref name="c">doi:10.1093/jmcb/mjp038</ref> and te Velthius A.J. ''et al'' (2007) <ref name="d">DOI 10.1100/tsw.2007.232</ref>.
@@ Line 44: / Line 44: @@
 ==Pathology==
-Deficiency in cardiac development and cardiac malfunction resulting from mutation and genetic studies have been identified within the ALP subfamily<ref name="d">DOI 10.1100/tsw.2007.232</ref>, <ref name="c">doi:10.1093/jmcb/mjp038</ref>. Human PDLIM2 (mystique) selectively interacts with highly pathogenic bird flu virus strain H5N1 via its PDZ domain, and as PDLIM2 is localised to the human cardiac muscle, this interaction speculatively tethers the pathogenic viral protein to the heart thereby mediating cardiac dysfunction likely with lethal effects associated to the pathogenic bird flu virus.
+Deficiency in cardiac development and cardiac malfunction resulting from mutation and genetic studies have been identified within the ALP subfamily<ref name="d">DOI 10.1100/tsw.2007.232</ref>, <ref name="c">doi:10.1093/jmcb/mjp038</ref>. Human PDLIM2 (mystique) selectively interacts with highly pathogenic bird flu virus strain H5N1 via its PDZ domain, and as PDLIM2 is localised to the human cardiac muscle, this interaction speculatively tethers the pathogenic viral protein to the heart thereby mediating cardiac dysfunction likely with lethal effects associated to the bird flu virus.