4oh9 - Revision history

OCA at 17:14, 20 September 2023

2023-09-20T17:14:01Z

←Older revision		Revision as of 17:14, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4oh9]] 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=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4oh9]] 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=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>
-	</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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [https://pdbe.org/4oh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 ProSAT]</span></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]] 1.699Å</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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [https://pdbe.org/4oh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:26, 25 January 2023

2023-01-25T07:26:16Z

←Older revision		Revision as of 07:26, 25 January 2023
Line 3:		Line 3:
	<StructureSection load='4oh9' size='340' side='right'caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4oh9' size='340' side='right'caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4oh9]] 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=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4oh9]] 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=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>~~	+	</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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [https://pdbe.org/4oh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">STK3, KRS1, MST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [~~http~~://pdbe.org/4oh9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/STK3_HUMAN STK3_HUMAN]] Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.<ref>PMID:8566796</ref> <ref>PMID:8816758</ref> <ref>PMID:15688006</ref> <ref>PMID:16930133</ref> <ref>PMID:18328708</ref> <ref>PMID:18362890</ref> <ref>PMID:19525978</ref> <ref>PMID:20212043</ref> <ref>PMID:21076410</ref> <ref>PMID:21104395</ref>	+	[https://www.uniprot.org/uniprot/STK3_HUMAN STK3_HUMAN] Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.<ref>PMID:8566796</ref> <ref>PMID:8816758</ref> <ref>PMID:15688006</ref> <ref>PMID:16930133</ref> <ref>PMID:18328708</ref> <ref>PMID:18362890</ref> <ref>PMID:19525978</ref> <ref>PMID:20212043</ref> <ref>PMID:21076410</ref> <ref>PMID:21104395</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 19:

	==See Also==		==See Also==
-	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]	+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Cheong C]]
-	[[Category: Cheong, C]]	+	[[Category: Cheong H-K]]
-	[[Category: Cheong, H K]]	+	[[Category: Hwang E]]
-	[[Category: Hwang, E]]	+	[[Category: Hwang KY]]
-	[[Category: Hwang~~, K Y~~]]	+	[[Category: Jeon YH]]
-	[[Category: Jeon~~, Y H~~]]	+	[[Category: Kim E]]
-	[[Category: Kim, E]]	+	[[Category: Kim H-Y]]
-	[[Category: Kim, H Y]]	+	[[Category: Lee WC]]
-	[[Category: Lee~~, W C~~]]	+	[[Category: Ul Mushtaq A]]
-	[[Category: Mushtaq, A Ul]]	+	[[Category: Yeo KJ]]
-	[[Category: Yeo~~, K J]]~~	+
-	~~[[Category: Coiled-coil]]~~	+
-	~~[[Category: Heterodimerization]]~~	+
-	~~[[Category: Homodierizarion]]~~	+
-	~~[[Category: Sarah domain]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:47, 17 April 2019

2019-04-17T07:47:50Z

←Older revision		Revision as of 07:47, 17 April 2019
Line 1:		Line 1:

	==Crystal Structure of the human MST2 SARAH homodimer==		==Crystal Structure of the human MST2 SARAH homodimer==
-	<StructureSection load='4oh9' size='340' side='right' caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4oh9' size='340' side='right'caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4oh9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4oh9]] 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=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">STK3, KRS1, MST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://pdbe.org/4oh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://pdbe.org/4oh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 ProSAT]</span></td></tr>
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Cheong, C]]		[[Category: Cheong, C]]

OCA at 00:31, 5 August 2016

2016-08-05T00:31:44Z

←Older revision		Revision as of 00:31, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the human MST2 SARAH homodimer==		==Crystal Structure of the human MST2 SARAH homodimer==
	<StructureSection load='4oh9' size='340' side='right' caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4oh9' size='340' side='right' caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://pdbe.org/4oh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4oh9" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine/threonine protein kinase\|Serine/threonine protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:12, 24 December 2014

2014-12-24T21:12:56Z

←Older revision		Revision as of 21:12, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4oh9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4oh9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 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=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/STK3_HUMAN STK3_HUMAN]] Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.<ref>PMID:8566796</ref> <ref>PMID:8816758</ref> <ref>PMID:15688006</ref> <ref>PMID:16930133</ref> <ref>PMID:18328708</ref> <ref>PMID:18362890</ref> <ref>PMID:19525978</ref> <ref>PMID:20212043</ref> <ref>PMID:21076410</ref> <ref>PMID:21104395</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 22:
	</StructureSection>		</StructureSection>
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Cheong, C.]]	+	[[Category: Cheong, C]]
-	[[Category: Cheong, H K.]]	+	[[Category: Cheong, H K]]
-	[[Category: Hwang, E.]]	+	[[Category: Hwang, E]]
-	[[Category: Hwang, K Y.]]	+	[[Category: Hwang, K Y]]
-	[[Category: Jeon, Y H.]]	+	[[Category: Jeon, Y H]]
-	[[Category: Kim, E.]]	+	[[Category: Kim, E]]
-	[[Category: Kim, H Y.]]	+	[[Category: Kim, H Y]]
-	[[Category: Lee, W C.]]	+	[[Category: Lee, W C]]
-	[[Category: Mushtaq, A Ul.]]	+	[[Category: Mushtaq, A Ul]]
-	[[Category: Yeo, K J.]]	+	[[Category: Yeo, K J]]
	[[Category: Coiled-coil]]		[[Category: Coiled-coil]]
	[[Category: Heterodimerization]]		[[Category: Heterodimerization]]

OCA at 07:51, 23 July 2014

2014-07-23T07:51:18Z

←Older revision		Revision as of 07:51, 23 July 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal Structure of the human MST2 SARAH homodimer==
		+	<StructureSection load='4oh9' size='340' side='right' caption='[[4oh9]], [[Resolution\|resolution]] 1.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4oh9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OH9 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4oh8\|4oh8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh9 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Despite recent progress in research on the Hippo signalling pathway, the structural information available in this area is extremely limited. Intriguingly, the homodimeric and heterodimeric interactions of mammalian sterile 20-like (MST) kinases through the so-called `SARAH' (SAV/RASSF/HPO) domains play a critical role in cellular homeostasis, dictating the fate of the cell regarding cell proliferation or apoptosis. To understand the mechanism of the heterodimerization of SARAH domains, the three-dimensional structures of an MST1-RASSF5 SARAH heterodimer and an MST2 SARAH homodimer were determined by X-ray crystallography and were analysed together with that previously determined for the MST1 SARAH homodimer. While the structure of the MST2 homodimer resembled that of the MST1 homodimer, the MST1-RASSF5 heterodimer showed distinct structural features. Firstly, the six N-terminal residues (Asp432-Lys437), which correspond to the short N-terminal 310-helix h1 kinked from the h2 helix in the MST1 homodimer, were disordered. Furthermore, the MST1 SARAH domain in the MST1-RASSF5 complex showed a longer helical structure (Ser438-Lys480) than that in the MST1 homodimer (Val441-Lys480). Moreover, extensive polar and nonpolar contacts in the MST1-RASSF5 SARAH domain were identified which strengthen the interactions in the heterodimer in comparison to the interactions in the homodimer. Denaturation experiments performed using urea also indicated that the MST-RASSF heterodimers are substantially more stable than the MST homodimers. These findings provide structural insights into the role of the MST1-RASSF5 SARAH domain in apoptosis signalling.

-	~~The entry 4oh9 is ON HOLD until Paper Publication~~	+	Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway.,Hwang E, Cheong HK, Mushtaq AU, Kim HY, Yeo KJ, Kim E, Lee WC, Hwang KY, Cheong C, Jeon YH Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):1944-53. doi:, 10.1107/S139900471400947X. Epub 2014 Jun 29. PMID:25004971<ref>PMID:25004971</ref>

-	~~Authors: Hwang~~, E., Cheong, H.-K., ~~Ul Mushtaq, A~~., ~~Kim, H.-~~Y., ~~Yeo, K~~.~~J.,~~ Kim, E., Lee, W.C., ~~Hwang~~, K.~~Y., Cheong, C., Jeon, Y.H.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal Structure of the human MST2 SARAH homodimer~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Cheong, C.]]
		+	[[Category: Cheong, H K.]]
		+	[[Category: Hwang, E.]]
		+	[[Category: Hwang, K Y.]]
		+	[[Category: Jeon, Y H.]]
		+	[[Category: Kim, E.]]
		+	[[Category: Kim, H Y.]]
		+	[[Category: Lee, W C.]]
		+	[[Category: Mushtaq, A Ul.]]
		+	[[Category: Yeo, K J.]]
		+	[[Category: Coiled-coil]]
		+	[[Category: Heterodimerization]]
		+	[[Category: Homodierizarion]]
		+	[[Category: Sarah domain]]
		+	[[Category: Transferase]]

OCA at 07:08, 29 January 2014

2014-01-29T07:08:21Z

←Older revision		Revision as of 07:08, 29 January 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4oh9 is ON HOLD	+	The entry 4oh9 is ON HOLD until Paper Publication

-	Authors: ~~Eunha~~ Hwang, ~~Hae-Kap~~ Cheong, ~~Ameeq~~ Ul Mushtaq, ~~Hye-Yeon~~ Kim, ~~Kwon Joo~~ Yeo, ~~Eunhee~~ Kim, ~~Woo Cheol~~ Lee, ~~Kwang Yeon~~ Hwang, ~~Chaejoon~~ Cheong, ~~Young Ho~~ Jeon	+	Authors: Hwang, E., Cheong, H.-K., Ul Mushtaq, A., Kim, H.-Y., Yeo, K.J., Kim, E., Lee, W.C., Hwang, K.Y., Cheong, C., Jeon, Y.H.

	Description: Crystal Structure of the human MST2 SARAH homodimer		Description: Crystal Structure of the human MST2 SARAH homodimer

OCA: Protected "4oh9" [edit=sysop:move=sysop]

2014-01-22T06:49:27Z

Protected "4oh9" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:49, 22 January 2014

OCA: New page: '''Unreleased structure''' The entry 4oh9 is ON HOLD Authors: Eunha Hwang, Hae-Kap Cheong, Ameeq Ul Mushtaq, Hye-Yeon Kim, Kwon Joo Yeo, Eunhee Kim, Woo Cheol Lee, Kwang Yeon Hwang, Cha...

2014-01-22T06:49:26Z

New page: '''Unreleased structure''' The entry 4oh9 is ON HOLD Authors: Eunha Hwang, Hae-Kap Cheong, Ameeq Ul Mushtaq, Hye-Yeon Kim, Kwon Joo Yeo, Eunhee Kim, Woo Cheol Lee, Kwang Yeon Hwang, Cha...

New page

'''Unreleased structure'''

The entry 4oh9 is ON HOLD

Authors: Eunha Hwang, Hae-Kap Cheong, Ameeq Ul Mushtaq, Hye-Yeon Kim, Kwon Joo Yeo, Eunhee Kim, Woo Cheol Lee, Kwang Yeon Hwang, Chaejoon Cheong, Young Ho Jeon

Description: Crystal Structure of the human MST2 SARAH homodimer