4r8g - Revision history

OCA at 08:59, 20 March 2024

2024-03-20T08:59:46Z

←Older revision		Revision as of 08:59, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 3.503Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [https://pdbe.org/4r8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [https://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g 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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [https://pdbe.org/4r8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [https://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation.		[https://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Class I myosins can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. How mechanical load is transduced from the membrane-binding tail to the force-generating head in myosin-1 is unknown. Here we determined the crystal structure of the entire tail of mouse myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable monomer conformation suited for force transduction. The lever-arm helix and the C-terminal extended PH domain of the motor are coupled by a stable post-IQ domain bound to calmodulin in a highly unusual mode. Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. Our study provides a structural blueprint for the neck and tail domains of myosin-1 and expands the target binding modes of the master Ca(2+)-signal regulator calmodulin.
-
-	Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.,Lu Q, Li J, Ye F, Zhang M Nat Struct Mol Biol. 2015 Jan;22(1):81-8. doi: 10.1038/nsmb.2923. Epub 2014 Dec, 1. PMID:25437912<ref>PMID:25437912</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4r8g" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 06:44, 2 March 2023

2023-03-02T06:44:12Z

←Older revision		Revision as of 06:44, 2 March 2023
Line 3:		Line 3:
	<StructureSection load='4r8g' size='340' side='right'caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='4r8g' size='340' side='right'caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~African_clawed_frog African clawed frog~~] and [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R8G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Myo1c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), calm1, calm2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [https://pdbe.org/4r8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [https://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g ProSAT]</span></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [~~http~~://pdbe.org/4r8g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.	+	[https://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: African clawed frog]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Li, J]]	+	[[Category: Xenopus laevis]]
-	[[Category: Lu, Q]]	+	[[Category: Li J]]
-	[[Category: Ye, F]]	+	[[Category: Lu Q]]
-	[[Category: Zhang, M]]	+	[[Category: Ye F]]
-	~~[[Category: Ca2+ signaling]]~~	+	[[Category: Zhang M]]
-	~~[[Category: Calcium binding]]~~	+
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Ef hand]]~~	+
-	~~[[Category: Force sensing]]~~	+
-	~~[[Category: Iq motif]]~~	+
-	~~[[Category: Lipid binding]]~~	+
-	~~[[Category: Myosin]]~~	+
-	~~[[Category: Ph domain]]~~	+
-	~~[[Category: Plasma membrane]]~~	+
-	~~[[Category: Protein binding-calcium-binding protein complex~~]]	+

OCA at 08:23, 18 December 2019

2019-12-18T08:23:36Z

←Older revision		Revision as of 08:23, 18 December 2019
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.		[[http://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Class I myosins can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. How mechanical load is transduced from the membrane-binding tail to the force-generating head in myosin-1 is unknown. Here we determined the crystal structure of the entire tail of mouse myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable monomer conformation suited for force transduction. The lever-arm helix and the C-terminal extended PH domain of the motor are coupled by a stable post-IQ domain bound to calmodulin in a highly unusual mode. Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. Our study provides a structural blueprint for the neck and tail domains of myosin-1 and expands the target binding modes of the master Ca(2+)-signal regulator calmodulin.
		+
		+	Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.,Lu Q, Li J, Ye F, Zhang M Nat Struct Mol Biol. 2015 Jan;22(1):81-8. doi: 10.1038/nsmb.2923. Epub 2014 Dec, 1. PMID:25437912<ref>PMID:25437912</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4r8g" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]		*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
-	*[[Myosin\|Myosin]]	+	*[[Myosin 3D Structures\|Myosin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:14, 1 May 2019

2019-05-01T10:14:39Z

←Older revision		Revision as of 10:14, 1 May 2019
Line 1:		Line 1:

	==Crystal Structure of Myosin-1c tail in complex with Calmodulin==		==Crystal Structure of Myosin-1c tail in complex with Calmodulin==
-	<StructureSection load='4r8g' size='340' side='right' caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>	+	<StructureSection load='4r8g' size='340' side='right'caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8G FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Myo1c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), calm1, calm2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://pdbe.org/4r8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g ProSAT]</span></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://pdbe.org/4r8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:

	==See Also==		==See Also==
-	*[[Calmodulin\|Calmodulin]]	+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
		+	*[[Myosin\|Myosin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: African clawed frog]]
		+	[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Li, J]]		[[Category: Li, J]]
	[[Category: Lu, Q]]		[[Category: Lu, Q]]

OCA at 14:01, 4 August 2016

2016-08-04T14:01:59Z

←Older revision		Revision as of 14:01, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Myosin-1c tail in complex with Calmodulin==		==Crystal Structure of Myosin-1c tail in complex with Calmodulin==
	<StructureSection load='4r8g' size='340' side='right' caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='4r8g' size='340' side='right' caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8G FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum]</span></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://pdbe.org/4r8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.		[[http://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
		+
		+	==See Also==
		+	*[[Calmodulin\|Calmodulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:23, 24 December 2014

2014-12-24T15:23:41Z

←Older revision		Revision as of 15:23, 24 December 2014
Line 6:		Line 6:
	<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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum]</span></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MYO1C_MOUSE MYO1C_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.<ref>PMID:16971510</ref> Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 09:43, 3 December 2014

2014-12-03T09:43:32Z

←Older revision		Revision as of 09:43, 3 December 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal Structure of Myosin-1c tail in complex with Calmodulin==
-		+	<StructureSection load='4r8g' size='340' side='right' caption='[[4r8g]], [[Resolution\|resolution]] 3.50Å' scene=''>
-	~~The entry~~ 4r8g is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4r8g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8G FirstGlance]. <br>
-	~~Authors~~: Lu, Q., Li, J., Ye, F., Zhang, M.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8g RCSB], [http://www.ebi.ac.uk/pdbsum/4r8g PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal Stucture of~~ Myosin	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Li, J]]
		+	[[Category: Lu, Q]]
		+	[[Category: Ye, F]]
		+	[[Category: Zhang, M]]
		+	[[Category: Ca2+ signaling]]
		+	[[Category: Calcium binding]]
		+	[[Category: Cytoskeleton]]
		+	[[Category: Ef hand]]
		+	[[Category: Force sensing]]
		+	[[Category: Iq motif]]
		+	[[Category: Lipid binding]]
		+	[[Category: Myosin]]
		+	[[Category: Ph domain]]
		+	[[Category: Plasma membrane]]
		+	[[Category: Protein binding-calcium-binding protein complex]]

OCA at 07:35, 5 November 2014

2014-11-05T07:35:48Z

←Older revision		Revision as of 07:35, 5 November 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4r8g is ON HOLD	+	The entry 4r8g is ON HOLD until Paper Publication

	Authors: Lu, Q., Li, J., Ye, F., Zhang, M.		Authors: Lu, Q., Li, J., Ye, F., Zhang, M.

	Description: Crystal Stucture of Myosin		Description: Crystal Stucture of Myosin

OCA: Protected "4r8g" [edit=sysop:move=sysop]

2014-09-10T08:25:56Z

Protected "4r8g" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:25, 10 September 2014

OCA: New page: '''Unreleased structure''' The entry 4r8g is ON HOLD Authors: Lu, Q., Li, J., Ye, F., Zhang, M. Description: Crystal Stucture of Myosin

2014-09-10T08:25:54Z

New page: '''Unreleased structure''' The entry 4r8g is ON HOLD Authors: Lu, Q., Li, J., Ye, F., Zhang, M. Description: Crystal Stucture of Myosin

New page

'''Unreleased structure'''

The entry 4r8g is ON HOLD

Authors: Lu, Q., Li, J., Ye, F., Zhang, M.

Description: Crystal Stucture of Myosin