5wj7 - Revision history

OCA at 14:14, 4 October 2023

2023-10-04T14:14:55Z

←Older revision		Revision as of 14:14, 4 October 2023
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	<StructureSection load='5wj7' size='340' side='right'caption='[[5wj7]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5wj7' size='340' side='right'caption='[[5wj7]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~MYH7~~, ~~MYHCB (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=~~5&~~id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5wj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj7 OCA], [~~http~~://pdbe.org/5wj7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5wj7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5wj7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj7 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj7 OCA], [https://pdbe.org/5wj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wj7 RCSB], [https://www.ebi.ac.uk/pdbsum/5wj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj7 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/MYH7_HUMAN MYH7_HUMAN] Defects in MYH7 are the cause of familial hypertrophic cardiomyopathy type 1 (CMH1) [MIM:[https://omim.org/entry/192600 192600]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:1975517</ref> <ref>PMID:1417858</ref> <ref>PMID:1638703</ref> <ref>PMID:1552912</ref> <ref>PMID:8250038</ref> <ref>PMID:8343162</ref> <ref>PMID:8435239</ref> <ref>PMID:8268932</ref> <ref>PMID:8254035</ref> <ref>PMID:8483915</ref> <ref>PMID:7848441</ref> <ref>PMID:7874131</ref> <ref>PMID:8282798</ref> <ref>PMID:7581410</ref> <ref>PMID:7731997</ref> <ref>PMID:8655135</ref> <ref>PMID:8899546</ref> <ref>PMID:10065021</ref> <ref>PMID:9544842</ref> <ref>PMID:9829907</ref> <ref>PMID:9822100</ref> <ref>PMID:10521296</ref> <ref>PMID:10563488</ref> <ref>PMID:10329202</ref> <ref>PMID:10679957</ref> <ref>PMID:10862102</ref> <ref>PMID:11113006</ref> <ref>PMID:11214007</ref> <ref>PMID:11733062</ref> <ref>PMID:11424919</ref> <ref>PMID:11133230</ref> <ref>PMID:12081993</ref> <ref>PMID:11861413</ref> <ref>PMID:11968089</ref> <ref>PMID:12951062</ref> <ref>PMID:12566107</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:12820698</ref> <ref>PMID:12975413</ref> <ref>PMID:12590187</ref> <ref>PMID:12818575</ref> <ref>PMID:15358028</ref> <ref>PMID:15563892</ref> <ref>PMID:15483641</ref> <ref>PMID:15858117</ref> <ref>PMID:16199542</ref> <ref>PMID:15856146</ref> <ref>PMID:16650083</ref> <ref>PMID:16938236</ref> <ref>PMID:17372140</ref> <ref>PMID:18403758</ref> Defects in MYH7 are the cause of myopathy myosin storage (MYOMS) [MIM:[https://omim.org/entry/608358 608358]. In this disorder, muscle biopsy shows type 1 fiber predominance and increased interstitial fat and connective tissue. Inclusion bodies consisting of the beta cardiac myosin heavy chain are present in the majority of type 1 fibers, but not in type 2 fibers.<ref>PMID:14520662</ref> <ref>PMID:15136674</ref> <ref>PMID:17336526</ref> Defects in MYH7 are the cause of scapuloperoneal myopathy MYH7-related (SPMM) [MIM:[https://omim.org/entry/181430 181430]; also known as scapuloperoneal syndrome myopathic type. SPMM is a progressive muscular atrophia beginning in the lower legs and affecting the shoulder region earlier and more severely than distal arm.<ref>PMID:17336526</ref> Defects in MYH7 are a cause of cardiomyopathy dilated type 1S (CMD1S) [MIM:[https://omim.org/entry/613426 613426]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11106718</ref> <ref>PMID:12379228</ref> <ref>PMID:15769782</ref> <ref>PMID:21846512</ref> Defects in MYH7 are the cause of myopathy distal type 1 (MPD1) [MIM:[https://omim.org/entry/160500 160500]. MPD1 is a muscular disorder characterized by early-onset selective weakness of the great toe and ankle dorsiflexors, followed by weakness of the finger extensors. Mild proximal weakness occasionally develops years later after the onset of the disease.<ref>PMID:15322983</ref> <ref>PMID:17548557</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/XRCC4_HUMAN XRCC4_HUMAN]] Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.<ref>PMID:8548796</ref> <ref>PMID:10854421</ref> <ref>PMID:10757784</ref> <ref>PMID:16412978</ref>	+	[https://www.uniprot.org/uniprot/XRCC4_HUMAN XRCC4_HUMAN] Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.<ref>PMID:8548796</ref> <ref>PMID:10854421</ref> <ref>PMID:10757784</ref> <ref>PMID:16412978</ref> [https://www.uniprot.org/uniprot/MYH7_HUMAN MYH7_HUMAN] Muscle contraction.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ajay, G]]	+	[[Category: Ajay G]]
-	[[Category: Andreas~~, M P~~]]	+	[[Category: Andreas MP]]
-	[[Category: Gellings, J]]	+	[[Category: Gellings J]]
-	[[Category: Rayment, I]]	+	[[Category: Rayment I]]
-	~~[[Category: Actin-dna binding protein complex]]~~	+
-	~~[[Category: Coiled-coil]]~~	+
-	~~[[Category: Myosin]]~~	+
-	~~[[Category: Xrcc4~~]]	+

OCA at 09:41, 4 December 2019

2019-12-04T09:41:47Z

←Older revision		Revision as of 09:41, 4 December 2019
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	==Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Xrcc4==		==Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Xrcc4==
-	<StructureSection load='5wj7' size='340' side='right' caption='[[5wj7]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='5wj7' size='340' side='right'caption='[[5wj7]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ajay, G]]		[[Category: Ajay, G]]
	[[Category: Andreas, M P]]		[[Category: Andreas, M P]]

OCA at 08:56, 27 December 2017

2017-12-27T08:56:17Z

←Older revision		Revision as of 08:56, 27 December 2017
Line 3:		Line 3:
	<StructureSection load='5wj7' size='340' side='right' caption='[[5wj7]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5wj7' size='340' side='right' caption='[[5wj7]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj7 OCA], [http://pdbe.org/5wj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wj7 RCSB], [http://www.ebi.ac.uk/pdbsum/5wj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj7 ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MYH7, MYHCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj7 OCA], [http://pdbe.org/5wj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wj7 RCSB], [http://www.ebi.ac.uk/pdbsum/5wj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Ajay, G]]		[[Category: Ajay, G]]
	[[Category: Andreas, M P]]		[[Category: Andreas, M P]]

OCA: Protected "5wj7" [edit=sysop:move=sysop]

2017-08-09T09:02:57Z

Protected "5wj7" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:02, 9 August 2017

OCA: New page: ==Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Xrcc4== == Structural highlights ==
<table><tr><td colspan='2'>[[5wj7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WJ7 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wj7 OCA], [http://pdbe.org/5wj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wj7 RCSB], [http://www.ebi.ac.uk/pdbsum/5wj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wj7 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/XRCC4_HUMAN XRCC4_HUMAN]] Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.<ref>PMID:8548796</ref> <ref>PMID:10854421</ref> <ref>PMID:10757784</ref> <ref>PMID:16412978</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
X-ray structural determination of segments of the myosin rod has proved difficult because of the strong salt-dependent aggregation properties and repeating pattern of charges on the surface of the coiled-coil that lead to the formation of paracrystals. This problem has been resolved in part through the use of globular assembly domains that improve protein folding and prevent aggregation. The primary consideration now in designing coiled-coil fusion constructs for myosin is deciding where to truncate the coiled-coil and which amino acid residues to include from the folding domain. This is especially important for myosin that contains numerous regions of low predicted coiled-coil propensity. Here we describe the strategy adopted to determine the structure of the region that extends from Arg1677 - Leu1797 that included two areas that do not show a strong sequence signature of a conventional left-handed coiled coil or canonical heptad repeat. This demonstrates again that, with careful choice of fusion constructs, overlapping structures exhibit very similar conformations for the myosin rod fragments in the canonical regions. However, conformational variability is seen around Leu1706 which is a hot spot for cardiomyopathy mutations suggesting that this might be important for function.

Design Considerations in Coiled-Coil Fusion Constructs for the Structural Determination of a Problematic Region of the Human Cardiac Myosin Rod.,Andreas MP, Ajay G, Gellings JA, Rayment I J Struct Biol. 2017 Jul 22. pii: S1047-8477(17)30120-X. doi:, 10.1016/j.jsb.2017.07.006. PMID:28743637<ref>PMID:28743637</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wj7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Ajay, G]]
[[Category: Andreas, M P]]
[[Category: Gellings, J]]
[[Category: Rayment, I]]
[[Category: Actin-dna binding protein complex]]
[[Category: Coiled-coil]]
[[Category: Myosin]]
[[Category: Xrcc4]]