6p59 - Revision history

OCA at 07:23, 11 October 2023

OCA — Wed, 11 Oct 2023 07:23:19 GMT

←Older revision		Revision as of 07:23, 11 October 2023
Line 3:		Line 3:
	<StructureSection load='6p59' size='340' side='right'caption='[[6p59]], [[Resolution\|resolution]] 2.94Å' scene=''>		<StructureSection load='6p59' size='340' side='right'caption='[[6p59]], [[Resolution\|resolution]] 2.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6p59]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P59 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6P59 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6p59]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Simian_immunodeficiency_virus Simian immunodeficiency virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P59 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.942214Å</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=6p59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p59 OCA], [~~http~~://pdbe.org/6p59 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6p59 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6p59 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6p59 ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6p59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p59 OCA], [https://pdbe.org/6p59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p59 RCSB], [https://www.ebi.ac.uk/pdbsum/6p59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p59 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/PEBB_HUMAN PEBB_HUMAN]] Note=A chromosomal aberration involving CBFB is associated with acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(p13;q22). The inversion produces a fusion protein that consists of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11.	+	[https://www.uniprot.org/uniprot/PEBB_HUMAN PEBB_HUMAN] Note=A chromosomal aberration involving CBFB is associated with acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(p13;q22). The inversion produces a fusion protein that consists of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PEBB_HUMAN PEBB_HUMAN]] CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBFB enhances DNA binding by RUNX1. [[http://www.uniprot.org/uniprot/ELOC_HUMAN ELOC_HUMAN]] SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).<ref>PMID:15590694</ref> The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.<ref>PMID:15590694</ref> [[http://www.uniprot.org/uniprot/ELOB_HUMAN ELOB_HUMAN]] SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).<ref>PMID:7638163</ref> <ref>PMID:15590694</ref> The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.<ref>PMID:7638163</ref> <ref>PMID:15590694</ref>	+	[https://www.uniprot.org/uniprot/PEBB_HUMAN PEBB_HUMAN] CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBFB enhances DNA binding by RUNX1.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 6p59" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6p59" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Core-binding factor\|Core-binding factor]]
		+	*[[Elongation factor 3D structures\|Elongation factor 3D structures]]
		+	*[[Virion infectivity factor\|Virion infectivity factor]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Binning, J M~~]]	+	[[Category: Simian immunodeficiency virus]]
-	[[Category: ~~Chesarino, N M~~]]	+	[[Category: Binning JM]]
-	[[Category: ~~Emerman, M~~]]	+	[[Category: Chesarino NM]]
-	[[Category: ~~Gross, J D~~]]	+	[[Category: Emerman M]]
-	[[Category: ~~A3g]]~~	+	[[Category: Gross JD]]
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Vif]]~~	+
-	~~[[Category: Viral protein]]~~	+
-	~~[[Category: Viral protein-immune system complex~~]]	+

OCA at 09:10, 25 December 2019

OCA — Wed, 25 Dec 2019 09:10:22 GMT

←Older revision		Revision as of 09:10, 25 December 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6p59 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of SIVrcm Vif-CBFbeta-ELOB-ELOC complex==
		+	<StructureSection load='6p59' size='340' side='right'caption='[[6p59]], [[Resolution\|resolution]] 2.94Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6p59]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P59 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6p59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p59 OCA], [http://pdbe.org/6p59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p59 RCSB], [http://www.ebi.ac.uk/pdbsum/6p59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p59 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PEBB_HUMAN PEBB_HUMAN]] Note=A chromosomal aberration involving CBFB is associated with acute myeloid leukemia of M4EO subtype. Pericentric inversion inv(16)(p13;q22). The inversion produces a fusion protein that consists of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PEBB_HUMAN PEBB_HUMAN]] CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBFB enhances DNA binding by RUNX1. [[http://www.uniprot.org/uniprot/ELOC_HUMAN ELOC_HUMAN]] SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).<ref>PMID:15590694</ref> The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.<ref>PMID:15590694</ref> [[http://www.uniprot.org/uniprot/ELOB_HUMAN ELOB_HUMAN]] SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).<ref>PMID:7638163</ref> <ref>PMID:15590694</ref> The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.<ref>PMID:7638163</ref> <ref>PMID:15590694</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Primate lentiviruses encode a Vif protein that counteracts the host antiviral APOBEC3 (A3) family members. The adaptation of Vif to species-specific A3 determinants is a critical event that allowed the spillover of a lentivirus from monkey reservoirs to chimpanzees and subsequently to humans, which gave rise to HIV-1 and the acquired immune deficiency syndrome (AIDS) pandemic. How Vif-A3 protein interactions are remodeled during evolution is unclear. Here, we report a 2.94 A crystal structure of the Vif substrate receptor complex from simian immunodeficiency virus isolated from red-capped mangabey (SIVrcm). The structure of the SIVrcm Vif complex illuminates the stage of lentiviral Vif evolution that is immediately prior to entering hominid primates. Structure-function studies reveal the adaptations that allowed SIVrcm Vif to antagonize hominid A3G. These studies show a partitioning between an evolutionarily dynamic specificity determinant and a conserved protein interacting surface on Vif that enables adaptation while maintaining protein interactions required for potent A3 antagonism.

-	~~Authors~~:	+	Structural Basis for a Species-Specific Determinant of an SIV Vif Protein toward Hominid APOBEC3G Antagonism.,Binning JM, Chesarino NM, Emerman M, Gross JD Cell Host Microbe. 2019 Dec 11;26(6):739-747.e4. doi: 10.1016/j.chom.2019.10.014. PMID:31830442<ref>PMID:31830442</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6p59" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Binning, J M]]
		+	[[Category: Chesarino, N M]]
		+	[[Category: Emerman, M]]
		+	[[Category: Gross, J D]]
		+	[[Category: A3g]]
		+	[[Category: Complex]]
		+	[[Category: Vif]]
		+	[[Category: Viral protein]]
		+	[[Category: Viral protein-immune system complex]]

OCA at 04:14, 19 June 2019

OCA — Wed, 19 Jun 2019 04:14:22 GMT

←Older revision		Revision as of 04:14, 19 June 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6p59 is ON HOLD	+	The entry 6p59 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6p59" [edit=sysop:move=sysop]

OCA — Wed, 05 Jun 2019 21:15:52 GMT

Protected "6p59" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:15, 5 June 2019

OCA: New page: '''Unreleased structure''' The entry 6p59 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 05 Jun 2019 21:15:50 GMT

New page: '''Unreleased structure''' The entry 6p59 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6p59 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]