Group:MUZIC:Enigma Family: Difference between revisions

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==Structure==

~~Atomic~~ structures of PDZ domain(s) of ~~Enigma subfamily members~~ have recently been solved. Likewise, the LIM-1 domain of Enigma Homologue protein has yielded its structure in atomic details~~; structural~~ models are depicted below from left to right.

Molecular structures of PDZ domain(s) of the three member proteins have recently been solved. Likewise, the LIM-1 domain of Enigma Homologue protein has yielded its structure in atomic details. Structural models are depicted below from left to right.

All structures revealed a canonical PDZ-domain fold containing six strands and 2 helices, except the '''PDZ domain of ZASP''' which has an extra helix between the third and fourth strand.

All member protein structures revealed canonical PDZ-domain structural fold containing six β-strands and 2 α-helices [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY], except the '''PDZ domain of ZASP''' which has an extra α-helix between the third and fourth β-strand.

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In general, the PDZ domain(s) of Enigma subfamily have been structurally revealed as a classical

class I PDZ domain - this is ~~further~~ suggested by its interaction with

class I PDZ domain - this is suggested by its interaction with

the C-terminal region of α-actinin-2 <ref>PMID:15062084</ref>. Recently, it has been shown that the PDZ domains of Enigma subfamily proteins

also interacts with Myotilin and Calsarcin/FATZ C-terminal

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factors. This common structural feature supports the notion that Enigma proteins serve as adaptor proteins, where the

PDZ domain tethers the protein to the cytoskeleton and the LIM

domain or additional internal domains (ZM-motif), recruit signaling proteins to implement corresponding functions (see <ref>doi:10.1093/jmcb/mjp038</ref>, and references therein). In addition, experimental evidences indicate Enigma protein may function as a scaffold on which the coordinated assembly of sarcomeric proteins can occur; largely owing to the interactions via its PDZ- and LIM domains with actin-associated proteins of cardiac and skeletal muscle, as well as non-muscle tissues [[<ref>PMID:7929196</ref>]]. It has also been implicated in bone formation and fracture repair<ref>PMID:11874232</ref>. It may also be involved in BMP6 signaling pathway. Generally, it interacts with various PKC isoforms using the LIM domains<ref>PMID:8940095</ref>. The LIM-2 domain has been shown to interact with TBX4, as well as RET in a phosphorylation-independent manner<ref>PMID:9528800</ref>. Despite the ~~colocalization~~ of '''Enigma protein''' with proteins in the Z-line and I-band, a definite functional role in the sarcomere has not

domain or additional internal domains (ZM-motif), recruit signaling proteins to implement corresponding functions (see <ref>doi:10.1093/jmcb/mjp038</ref>, and references therein). In addition, experimental evidences indicate Enigma protein may function as a scaffold on which the coordinated assembly of sarcomeric proteins can occur; largely owing to the interactions via its PDZ- and LIM domains with actin-associated proteins of cardiac and skeletal muscle, as well as non-muscle tissues [[<ref>PMID:7929196</ref>]]. It has also been implicated in bone formation and fracture repair<ref>PMID:11874232</ref>. It may also be involved in BMP6 signaling pathway. Generally, it interacts with various PKC isoforms using the LIM domains<ref>PMID:8940095</ref>. The LIM-2 domain has been shown to interact with TBX4, as well as RET in a phosphorylation-independent manner<ref>PMID:9528800</ref>. Despite the co-localization of '''Enigma protein''' with proteins in the Z-line and I-band, a definite functional role in the sarcomere has not

been shown yet<ref>doi:10.1093/jmcb/mjp038</ref>; '''''which resounds the literal meaning of the word Enigma'''.''

@@ Line 23: / Line 23: @@
 ==Structure==
-Atomic structures of PDZ domain(s) of Enigma subfamily members have recently been solved. Likewise, the LIM-1 domain of Enigma Homologue protein has yielded its structure in atomic details; structural models are depicted below from left to right.
+Molecular structures of PDZ domain(s) of the three member proteins have recently been solved. Likewise, the LIM-1 domain of Enigma Homologue protein has yielded its structure in atomic details. Structural models are depicted below from left to right.
-All structures revealed a canonical PDZ-domain fold containing six strands and 2 helices, except the '''PDZ domain of ZASP''' which has an extra helix between the third and fourth strand.
+All member protein structures revealed canonical PDZ-domain structural fold containing six β-strands and 2 α-helices [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY], except the '''PDZ domain of ZASP''' which has an extra α-helix between the third and fourth β-strand.
-<Structure load='PDLIM7.pdb' size='250' frame='true' align='left' caption='X-ray crystal structure of PDZ domain of Enigma protein at 1.11Å (Adapted PDB ID: 2Q3G [http://www.rcsb.org/pdb/explore/explore.do?structureId=2Q3G)]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Pdz_enigma/3'/>
+<Structure load='PDLIM7.pdb' size='250' frame='true' align='left' caption='X-ray crystal structure of PDZ domain of Enigma protein at 1.11Å (PDB ID: 2Q3G [http://www.rcsb.org/pdb/explore/explore.do?structureId=2Q3G)]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Pdz_enigma/3'/>
 <Structure load='ENH_PDZ.pdb' size='250' frame='true' align='left' caption='NMR solution structure of PDZ domain of Enigma Homologue protein (PDB ID: 1WF7) [http://www.rcsb.org/pdb/explore/explore.do?structureId=1WF7]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_pdz/5' />
@@ Line 69: / Line 69: @@
 In general, the PDZ domain(s) of Enigma subfamily have been structurally revealed as a classical
-class I PDZ domain - this is further suggested by its interaction with
+class I PDZ domain - this is suggested by its interaction with
 the C-terminal region of α-actinin-2 <ref>PMID:15062084</ref>. Recently, it has been shown that the PDZ domains of Enigma subfamily proteins
 also interacts with Myotilin and Calsarcin/FATZ C-terminal
@@ Line 77: / Line 77: @@
 factors. This common structural feature supports the notion that Enigma proteins serve as adaptor proteins, where the
 PDZ domain tethers the protein to the cytoskeleton and the LIM
-domain or additional internal domains (ZM-motif), recruit signaling proteins to implement corresponding functions (see <ref>doi:10.1093/jmcb/mjp038</ref>, and references therein). In addition, experimental evidences indicate Enigma protein may function as a scaffold on which the coordinated assembly of sarcomeric proteins can occur; largely owing to the interactions via its PDZ- and LIM domains with actin-associated proteins of cardiac and skeletal muscle, as well as non-muscle tissues [[<ref>PMID:7929196</ref>]]. It has also been implicated in bone formation and fracture repair<ref>PMID:11874232</ref>. It may also be involved in BMP6 signaling pathway. Generally, it interacts with various PKC isoforms using the LIM domains<ref>PMID:8940095</ref>. The LIM-2 domain has been shown to interact with TBX4, as well as RET in a phosphorylation-independent manner<ref>PMID:9528800</ref>. Despite the colocalization of '''Enigma protein''' with proteins in the Z-line and I-band, a definite functional role in the sarcomere has not
+domain or additional internal domains (ZM-motif), recruit signaling proteins to implement corresponding functions (see <ref>doi:10.1093/jmcb/mjp038</ref>, and references therein). In addition, experimental evidences indicate Enigma protein may function as a scaffold on which the coordinated assembly of sarcomeric proteins can occur; largely owing to the interactions via its PDZ- and LIM domains with actin-associated proteins of cardiac and skeletal muscle, as well as non-muscle tissues [[<ref>PMID:7929196</ref>]]. It has also been implicated in bone formation and fracture repair<ref>PMID:11874232</ref>. It may also be involved in BMP6 signaling pathway. Generally, it interacts with various PKC isoforms using the LIM domains<ref>PMID:8940095</ref>. The LIM-2 domain has been shown to interact with TBX4, as well as RET in a phosphorylation-independent manner<ref>PMID:9528800</ref>. Despite the co-localization of '''Enigma protein''' with proteins in the Z-line and I-band, a definite functional role in the sarcomere has not
 been shown yet<ref>doi:10.1093/jmcb/mjp038</ref>; '''''which resounds the literal meaning of the word Enigma'''.''