Group:MUZIC:Enigma Family - Revision history

Michal Harel at 09:38, 3 February 2016

Michal Harel — Wed, 03 Feb 2016 09:38:09 GMT

←Older revision		Revision as of 09:38, 3 February 2016
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	==Structure==		==Structure==

-	<Structure load='LIM1.pdb' size='200' frame='true' align='right' caption='NMR solution structure of LIM-1 domain of Enigma Homologue protein (PDB ID: ~~2DAR~~) [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DAR]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_lim1/2' />	+	<Structure load='LIM1.pdb' size='200' frame='true' align='right' caption='NMR solution structure of LIM-1 domain of Enigma Homologue protein (PDB ID: [[2dar]]) [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DAR]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_lim1/2' />

-	<Structure load='PDLIM7.pdb' size='200' frame='true' align='right' 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='PDLIM7.pdb' size='200' frame='true' align='right' 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'/>

	'''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY]		'''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY]

Adekunle Onipe: /* Pathology */

Adekunle Onipe — Thu, 16 Jul 2015 01:07:34 GMT

Pathology

←Older revision		Revision as of 01:07, 16 July 2015
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	==Pathology==		==Pathology==
-	Mutations in the '''ZASP''' gene have been associated with dilated cardiomyopathy (DCM) and DCM	+	Mutations in the '''[http://proteopedia.org/wiki/index.php/Group:MUZIC:ZASP ZASP]''' gene have been associated with dilated cardiomyopathy (DCM) and DCM
	associated with isolated left ventricular noncompaction of the myocardium (INLVM) in humans <ref>PMID:14662268</ref>.		associated with isolated left ventricular noncompaction of the myocardium (INLVM) in humans <ref>PMID:14662268</ref>.
	The presence of multiple mutations in the ZASP gene in patients		The presence of multiple mutations in the ZASP gene in patients
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	various regions of the brain, suggest a possible role in brain development<ref>PMID:12665800</ref>. In accordance, ENH		various regions of the brain, suggest a possible role in brain development<ref>PMID:12665800</ref>. In accordance, ENH
	expression levels were found to be significantly increased in all brain regions of patients with bipolar disorder, schizophrenia, and major depression(see <ref>DOI 10.1100/tsw.2007.232</ref>, and references therein).		expression levels were found to be significantly increased in all brain regions of patients with bipolar disorder, schizophrenia, and major depression(see <ref>DOI 10.1100/tsw.2007.232</ref>, and references therein).
-

	==References==		==References==
	<references/>		<references/>

Adekunle Onipe at 00:21, 16 July 2015

Adekunle Onipe — Thu, 16 Jul 2015 00:21:44 GMT

←Older revision		Revision as of 00:21, 16 July 2015
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	==Introduction==		==Introduction==

-	'''Enigma subfamily: PDZ/LIM-domain proteins of the cytoskeleton'''. Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice variants identified in the first member, a common feature in all member proteins, as well as their redundant, indinstinct functions in the cytoskeleton. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (domain named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (domain named after three proteins where it was first characterized '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The Enigma member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.	+	'''Enigma subfamily: PDZ/LIM-domain proteins of the cytoskeleton'''. Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''[http://proteopedia.org/wiki/index.php/Group:MUZIC:ZASP ZASP/Cypher/Oracle]''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice variants identified in the first member, a common feature in all member proteins, as well as their redundant, indinstinct functions in the cytoskeleton. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (domain named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (domain named after three proteins where it was first characterized '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The Enigma member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.

	==Sequence annotation==		==Sequence annotation==
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	'''ZASP''' [http://www.uniprot.org/uniprot/O75112#section_features)]'''ENH''' [http://www.uniprot.org/uniprot/Q96HC4#section_alternative]'''Enigma''' [http://www.uniprot.org/uniprot/Q9NR12#section_features]]]		'''ZASP''' [http://www.uniprot.org/uniprot/O75112#section_features)]'''ENH''' [http://www.uniprot.org/uniprot/Q96HC4#section_alternative]'''Enigma''' [http://www.uniprot.org/uniprot/Q9NR12#section_features]]]

-	'''ZASP''' ('''Z'''-disk '''A'''lternatively '''S'''pliced '''P'''DZ domain protein), also referred to as LIM domain-binding protein 3 (LDB-3), is the 78 kDa, 727-amino-acid human ortholog of cypher, independently identified in heart and skeletal	+	'''[http://proteopedia.org/wiki/index.php/Group:MUZIC:ZASP ZASP]''' ('''Z'''-disk '''A'''lternatively '''S'''pliced '''P'''DZ domain protein), also referred to as LIM domain-binding protein 3 (LDB-3), is the 78 kDa, 727-amino-acid human ortholog of cypher, independently identified in heart and skeletal
	muscle<ref>PMID:10427098</ref>. Five alternatively spliced isoforms of ZASP have been identified (UniProtKB: O75112)[http://www.uniprot.org/uniprot/O75112#section_features)]. Apart from the PDZ domain, ZASP possess an internal motif (ZASP-like motif) which confers the ability to interact with the spectrin repeats of α-actinin-2 <ref>doi:10.1016/j.yexcr.2005.12.036</ref>.		muscle<ref>PMID:10427098</ref>. Five alternatively spliced isoforms of ZASP have been identified (UniProtKB: O75112)[http://www.uniprot.org/uniprot/O75112#section_features)]. Apart from the PDZ domain, ZASP possess an internal motif (ZASP-like motif) which confers the ability to interact with the spectrin repeats of α-actinin-2 <ref>doi:10.1016/j.yexcr.2005.12.036</ref>.

Adekunle Onipe: /* Structure */

Adekunle Onipe — Wed, 10 Oct 2012 04:53:10 GMT

Structure

←Older revision		Revision as of 04:53, 10 October 2012
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	<Structure load='PDLIM7.pdb' size='200' frame='true' align='right' 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='PDLIM7.pdb' size='200' frame='true' align='right' 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'/>

-	'''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY]~~, except the '''PDZ domain of ZASP''' which has a short α-helix bridging the B and C β-strands.~~	+	'''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY]

	==Function and Interactions==		==Function and Interactions==

Adekunle Onipe at 04:52, 10 October 2012

Adekunle Onipe — Wed, 10 Oct 2012 04:52:01 GMT

←Older revision		Revision as of 04:52, 10 October 2012
Line 1:		Line 1:
-	==~~Enigma subfamily: PDZ/LIM-domain proteins of the cytoskeleton~~==	+	==Introduction==

-	Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice variants identified in the first member, a common feature in all member proteins, as well as their redundant, indinstinct functions in the cytoskeleton. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (domain named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (domain named after three proteins where it was first characterized '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The Enigma member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.	+	'''Enigma subfamily: PDZ/LIM-domain proteins of the cytoskeleton'''. Three member proteins have extensively been described and characterized within this subfamily: '''Enigma''' protein, '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle''' (ZASP<ref>PMID:10427098</ref> being the human orthologue of cypher<ref>PMID:10391924</ref> in mouse, also identified by independent researchers as oracle<ref>PMID:10727866</ref>). The family name - ''Enigma'' - possibly was inspired by the intricately complicated splice variants identified in the first member, a common feature in all member proteins, as well as their redundant, indinstinct functions in the cytoskeleton. Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (domain named after first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domains (domain named after three proteins where it was first characterized '''L'''in-11, '''I'''sl1 and '''M'''ec-3)<ref>PMID:20042479</ref>. The Enigma member proteins have all been located to the mammalian muscle cells, some specific to the heart and skeletal muscle Z-disk. They interact via their PDZ domains with protein components of the Z-disk and also recruit signalling molecules via their LIM domains or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP)<ref>doi:10.1161/CIRCRESAHA.110.225615</ref>. These interactions via their PDZ- and LIM-domains suggest roles important for targeting/sustaining interacting protein complexes within the myofibrillar sarcomere for a physiologically functional muscle.

-	==Sequence annotation ~~and domain organization~~==	+	==Sequence annotation==

	[[Image:Enigma_family.png\|left\|thumb\|450px\| PDZ- and LIM-domains map in the first isoforms of human Enigma subfamily members:		[[Image:Enigma_family.png\|left\|thumb\|450px\| PDZ- and LIM-domains map in the first isoforms of human Enigma subfamily members:
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	'''Enigma''' protein		'''Enigma''' protein
	alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref> <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified (UniProtKB ID: Q9NR12)[http://www.uniprot.org/uniprot/Q9NR12#section_features].		alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref> <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified (UniProtKB ID: Q9NR12)[http://www.uniprot.org/uniprot/Q9NR12#section_features].
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	==Structure==		==Structure==

Adekunle Onipe at 08:39, 16 December 2011

Adekunle Onipe — Fri, 16 Dec 2011 08:39:49 GMT

←Older revision		Revision as of 08:39, 16 December 2011
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	==Sequence annotation and domain organization==		==Sequence annotation and domain organization==

-	[[Image:Enigma_family.png\|~~right~~\|thumb\|450px\| PDZ- and LIM-domains map in the first isoforms of human Enigma subfamily members:	+	[[Image:Enigma_family.png\|left\|thumb\|450px\| PDZ- and LIM-domains map in the first isoforms of human Enigma subfamily members:
	'''ZASP''' [http://www.uniprot.org/uniprot/O75112#section_features)]'''ENH''' [http://www.uniprot.org/uniprot/Q96HC4#section_alternative]'''Enigma''' [http://www.uniprot.org/uniprot/Q9NR12#section_features]]]		'''ZASP''' [http://www.uniprot.org/uniprot/O75112#section_features)]'''ENH''' [http://www.uniprot.org/uniprot/Q96HC4#section_alternative]'''Enigma''' [http://www.uniprot.org/uniprot/Q9NR12#section_features]]]

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	'''Enigma''' protein		'''Enigma''' protein
	alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref> <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified (UniProtKB ID: Q9NR12)[http://www.uniprot.org/uniprot/Q9NR12#section_features].		alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref> <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified (UniProtKB ID: Q9NR12)[http://www.uniprot.org/uniprot/Q9NR12#section_features].
		+
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	==Structure==		==Structure==

Adekunle Onipe at 08:25, 9 December 2011

Adekunle Onipe — Fri, 09 Dec 2011 08:25:24 GMT

←Older revision		Revision as of 08:25, 9 December 2011
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	'''Enigma''' protein		'''Enigma''' protein
	alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref> <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified (UniProtKB ID: Q9NR12)[http://www.uniprot.org/uniprot/Q9NR12#section_features].		alternatively referred to as PDLIM7 (PDZ and LIM domain protein 7) is the first and representative member of the Enigma subfamily. Initially characterized in human as ~49.85 kDa, 457 amino-acid protein with an N-terminal PDZ domain and three C-terminal LIM domains <ref>PMID:7929196</ref> <ref>PMID:10359609</ref>. Five alternatively spliced isoforms are presently identified (UniProtKB ID: Q9NR12)[http://www.uniprot.org/uniprot/Q9NR12#section_features].
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	==Structure==		==Structure==
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	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		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'''.''		been shown yet<ref>doi:10.1093/jmcb/mjp038</ref>; '''''which resounds the literal meaning of the word Enigma'''.''
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	==Pathology==		==Pathology==

Adekunle Onipe at 11:33, 30 November 2011

Adekunle Onipe — Wed, 30 Nov 2011 11:33:55 GMT

←Older revision		Revision as of 11:33, 30 November 2011
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	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		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'''.''		been shown yet<ref>doi:10.1093/jmcb/mjp038</ref>; '''''which resounds the literal meaning of the word Enigma'''.''
		+
		+
		+
		+

	==Pathology==		==Pathology==

Adekunle Onipe: /* Structure */

Adekunle Onipe — Wed, 30 Nov 2011 11:32:39 GMT

Structure

←Older revision		Revision as of 11:32, 30 November 2011
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	==Structure==		==Structure==
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-	<Structure load='PDLIM7.pdb' size='200' frame='true' align='right' 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='200' frame='true' align='right' 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' />

	<Structure load='LIM1.pdb' size='200' frame='true' align='right' caption='NMR solution structure of LIM-1 domain of Enigma Homologue protein (PDB ID: 2DAR) [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DAR]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_lim1/2' />		<Structure load='LIM1.pdb' size='200' frame='true' align='right' caption='NMR solution structure of LIM-1 domain of Enigma Homologue protein (PDB ID: 2DAR) [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DAR]' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_lim1/2' />

-	<Structure load='~~1RGW~~' size='200' frame='true' align='right' caption='~~NMR solution~~ structure of PDZ domain of ~~ZASP~~ (PDB ID: ~~1RGW)~~ [http://www.rcsb.org/pdb/explore/explore.do?structureId=~~1RGW~~]' scene='User:Adekunle_Onipe/workbench/~~ZASP~~/~~Zasp_pdz_domain~~/3' /> '''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY], except the '''PDZ domain of ZASP''' which appears to have an extra α-helix bridging the B and C β-strands; even though this extra helix, when looked at from a distal orientation, appears to be a tandem/part of the canonical B α-helix.	+	<Structure load='PDLIM7.pdb' size='200' frame='true' align='right' 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'/>
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		+	'''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY], except the '''PDZ domain of ZASP''' which has a short α-helix bridging the B and C β-strands.

	==Function and Interactions==		==Function and Interactions==

Adekunle Onipe at 17:05, 22 July 2011

Adekunle Onipe — Fri, 22 Jul 2011 17:05:23 GMT

←Older revision		Revision as of 17:05, 22 July 2011
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	<Structure load='1RGW' size='200' frame='true' align='right' caption='NMR solution structure of PDZ domain of ZASP (PDB ID: 1RGW) [http://www.rcsb.org/pdb/explore/explore.do?structureId=1RGW]' scene='User:Adekunle_Onipe/workbench/ZASP/Zasp_pdz_domain/3' /> '''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY], except the '''PDZ domain of ZASP''' which appears to have an extra α-helix bridging the B and C β-strands; even though this extra helix, when looked at from a distal orientation, appears to be a tandem/part of the canonical B α-helix.		<Structure load='1RGW' size='200' frame='true' align='right' caption='NMR solution structure of PDZ domain of ZASP (PDB ID: 1RGW) [http://www.rcsb.org/pdb/explore/explore.do?structureId=1RGW]' scene='User:Adekunle_Onipe/workbench/ZASP/Zasp_pdz_domain/3' /> '''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 model of all member proteins reveal canonical PDZ domain fold containing six β-strands (A-F) and 2 α-helices (A and B) [http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=PDZ&BLAST=DUMMY], except the '''PDZ domain of ZASP''' which appears to have an extra α-helix bridging the B and C β-strands; even though this extra helix, when looked at from a distal orientation, appears to be a tandem/part of the canonical B α-helix.
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	==Function and Interactions==		==Function and Interactions==