6sho - Revision history

OCA at 11:51, 13 November 2019

OCA — Wed, 13 Nov 2019 11:51:12 GMT

←Older revision		Revision as of 11:51, 13 November 2019
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	<StructureSection load='6sho' size='340' side='right'caption='[[6sho]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='6sho' size='340' side='right'caption='[[6sho]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6sho]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SHO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6sho]] 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=6SHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SHO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BIRC5, API4, IAP4 ([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=6sho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sho OCA], [http://pdbe.org/6sho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sho RCSB], [http://www.ebi.ac.uk/pdbsum/6sho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sho 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=6sho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sho OCA], [http://pdbe.org/6sho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sho RCSB], [http://www.ebi.ac.uk/pdbsum/6sho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sho ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref>		[[http://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Single-wavelength X-ray anomalous diffraction (SAD) is a frequently employed technique to solve the phase problem in X-ray crystallography. The precision and accuracy of recovered anomalous differences are crucial for determining the correct phases. Continuous rotation (CR) and inverse-beam geometry (IBG) anomalous data collection methods have been performed on tetragonal lysozyme and monoclinic survivin crystals and analysis carried out of how correlated the pairs of Friedel's reflections are after scaling. A multivariate Bayesian model for estimating anomalous differences was tested, which takes into account the correlation between pairs of intensity observations and incorporates the a priori knowledge about the positivity of intensity. The CR and IBG data collection methods resulted in positive correlation between I(+) and I(-) observations, indicating that the anomalous difference dominates between these observations, rather than different levels of radiation damage. An alternative pairing method based on near simultaneously observed Bijvoet's pairs displayed lower correlation and it was unsuccessful for recovering useful anomalous differences when using the multivariate Bayesian model. In contrast, multivariate Bayesian treatment of Friedel's pairs improved the initial phasing of the two tested crystal systems and the two data collection methods.
		+
		+	Bayesian machine learning improves single-wavelength anomalous diffraction phasing.,Garcia-Bonete MJ, Katona G Acta Crystallogr A Found Adv. 2019 Nov 1;75(Pt 6):851-860. doi:, 10.1107/S2053273319011446. Epub 2019 Oct 7. PMID:31692460<ref>PMID:31692460</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6sho" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Garcia-Bonete, M J]]		[[Category: Garcia-Bonete, M J]]

OCA at 06:50, 6 November 2019

OCA — Wed, 06 Nov 2019 06:50:57 GMT

←Older revision		Revision as of 06:50, 6 November 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6sho is ~~ON HOLD until Paper Publication~~	+	==SAD structure of Human Survivin recovered by continuous rotation data collection and multivariate analysis of Friedel pairs==
-		+	<StructureSection load='6sho' size='340' side='right'caption='[[6sho]], [[Resolution\|resolution]] 3.20Å' scene=''>
-	~~Authors~~: ~~Garcia~~-~~Bonete~~, M.J., ~~Katona~~, G.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6sho]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SHO FirstGlance]. <br>
-	~~Description~~: ~~SAD structure~~ of ~~Human Survivin recovered by continuous rotation data collection~~ and ~~multivariate analysis~~ of ~~Friedel pairs~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<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=6sho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sho OCA], [http://pdbe.org/6sho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sho RCSB], [http://www.ebi.ac.uk/pdbsum/6sho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sho ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Garcia-Bonete, M J]]
	[[Category: Katona, G]]		[[Category: Katona, G]]
-	[[Category: ~~Garcia~~-~~Bonete, M.J~~]]	+	[[Category: Apoptosis]]
		+	[[Category: Continuous rotation]]
		+	[[Category: Human survivin]]
		+	[[Category: Multivariate analysis]]
		+	[[Category: Single-wavelength x-ray anomalous diffraction]]

OCA at 04:22, 16 October 2019

OCA — Wed, 16 Oct 2019 04:22:32 GMT

←Older revision		Revision as of 04:22, 16 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6sho is ON HOLD	+	The entry 6sho is ON HOLD until Paper Publication

	Authors: Garcia-Bonete, M.J., Katona, G.		Authors: Garcia-Bonete, M.J., Katona, G.

OCA: Protected "6sho" [edit=sysop:move=sysop]

OCA — Wed, 14 Aug 2019 15:14:55 GMT

Protected "6sho" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:14, 14 August 2019

OCA: New page: '''Unreleased structure''' The entry 6sho is ON HOLD Authors: Garcia-Bonete, M.J., Katona, G. Description: SAD structure of Human Survivin recovered by continuous rotation data collect...

OCA — Wed, 14 Aug 2019 15:14:54 GMT

New page: '''Unreleased structure''' The entry 6sho is ON HOLD Authors: Garcia-Bonete, M.J., Katona, G. Description: SAD structure of Human Survivin recovered by continuous rotation data collect...

New page

'''Unreleased structure'''

The entry 6sho is ON HOLD

Authors: Garcia-Bonete, M.J., Katona, G.

Description: SAD structure of Human Survivin recovered by continuous rotation data collection and multivariate analysis of Friedel pairs
[[Category: Unreleased Structures]]
[[Category: Katona, G]]
[[Category: Garcia-Bonete, M.J]]