4a0c - Revision history

OCA at 11:17, 20 December 2023

OCA — Wed, 20 Dec 2023 11:17:24 GMT

←Older revision		Revision as of 11:17, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='4a0c' size='340' side='right'caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>		<StructureSection load='4a0c' size='340' side='right'caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~] and [https://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=4A0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A0C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A0C FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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]] 3.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1u6g\|1u6g]], [[4a0l\|4a0l]], [[4a0k\|4a0k]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [https://pdbe.org/4a0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [https://www.ebi.ac.uk/pdbsum/4a0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0c 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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [https://pdbe.org/4a0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [https://www.ebi.ac.uk/pdbsum/4a0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0c ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[https://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[https://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref> <ref>PMID:20002452</ref> <ref>PMID:17236139</ref> <ref>PMID:19377476</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref> [[https://www.uniprot.org/uniprot/RBX1_MOUSE RBX1_MOUSE]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity).<ref>PMID:12140560</ref> [[https://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref> <ref>PMID:16322693</ref> <ref>PMID:16678110</ref> <ref>PMID:18593899</ref> <ref>PMID:18235224</ref> <ref>PMID:19801544</ref>	+	[https://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Faty, M]]	+	[[Category: Faty M]]
-	[[Category: Fischer~~, E S~~]]	+	[[Category: Fischer ES]]
-	[[Category: Gut, H]]	+	[[Category: Gut H]]
-	[[Category: Scrima, A]]	+	[[Category: Scrima A]]
-	[[Category: Thoma~~, N H]]~~	+	[[Category: Thoma NH]]
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Dna damage repair]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Ubiquitin~~]]	+

OCA at 07:36, 18 August 2022

OCA — Thu, 18 Aug 2022 07:36:35 GMT

←Older revision		Revision as of 07:36, 18 August 2022
Line 3:		Line 3:
	<StructureSection load='4a0c' size='340' side='right'caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>		<StructureSection load='4a0c' size='340' side='right'caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human] 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=4A0C OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4A0C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://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=4A0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A0C 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" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u6g\|1u6g]], [[4a0l\|4a0l]], [[4a0k\|4a0k]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u6g\|1u6g]], [[4a0l\|4a0l]], [[4a0k\|4a0k]]</div></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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [~~http~~://pdbe.org/4a0c PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4a0c PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0c 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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [https://pdbe.org/4a0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [https://www.ebi.ac.uk/pdbsum/4a0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0c ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[~~http~~://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref> <ref>PMID:20002452</ref> <ref>PMID:17236139</ref> <ref>PMID:19377476</ref>	+	[[https://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[https://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref> <ref>PMID:20002452</ref> <ref>PMID:17236139</ref> <ref>PMID:19377476</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref> [[~~http~~://www.uniprot.org/uniprot/RBX1_MOUSE RBX1_MOUSE]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity).<ref>PMID:12140560</ref> [[~~http~~://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref> <ref>PMID:16322693</ref> <ref>PMID:16678110</ref> <ref>PMID:18593899</ref> <ref>PMID:18235224</ref> <ref>PMID:19801544</ref>	+	[[https://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref> [[https://www.uniprot.org/uniprot/RBX1_MOUSE RBX1_MOUSE]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity).<ref>PMID:12140560</ref> [[https://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref> <ref>PMID:16322693</ref> <ref>PMID:16678110</ref> <ref>PMID:18593899</ref> <ref>PMID:18235224</ref> <ref>PMID:19801544</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Cullin\|Cullin]]	+	*[[Cullin 3D structures\|Cullin 3D structures]]
-	*[[~~RING~~ box protein\|~~RING~~ box protein]]	+	*[[Ring box protein 3D structures\|Ring box protein 3D structures]]
-	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]	+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:41, 3 April 2019

OCA — Wed, 03 Apr 2019 07:41:37 GMT

←Older revision		Revision as of 07:41, 3 April 2019
Line 1:		Line 1:

	==Structure of the CAND1-CUL4B-RBX1 complex==		==Structure of the CAND1-CUL4B-RBX1 complex==
-	<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>	+	<StructureSection load='4a0c' size='340' side='right'caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=4A0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A0C FirstGlance]. <br>		<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=4A0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A0C FirstGlance]. <br>
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4a0c" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4a0c" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cullin\|Cullin]]
		+	*[[RING box protein\|RING box protein]]
		+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Faty, M]]		[[Category: Faty, M]]

OCA at 22:09, 15 November 2017

OCA — Wed, 15 Nov 2017 22:09:56 GMT

←Older revision		Revision as of 22:09, 15 November 2017
Line 1:		Line 1:

-	==~~STRUCTURE OF THE~~ CAND1-CUL4B-RBX1 ~~COMPLEX~~==	+	==Structure of the CAND1-CUL4B-RBX1 complex==
	<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>		<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4a0c" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4a0c" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cullin\|Cullin]]
-	*[[RING box protein\|RING box protein]]
-	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:15, 5 August 2016

OCA — Fri, 05 Aug 2016 14:15:43 GMT

←Older revision		Revision as of 14:15, 5 August 2016
Line 1:		Line 1:
		+
	==STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX==		==STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX==
	<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>		<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~] and [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A0C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=4A0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A0C 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u6g\|1u6g]], [[4a0l\|4a0l]], [[4a0k\|4a0k]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u6g\|1u6g]], [[4a0l\|4a0l]], [[4a0k\|4a0k]]</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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [http://www.ebi.ac.uk/pdbsum/4a0c 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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [http://pdbe.org/4a0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [http://www.ebi.ac.uk/pdbsum/4a0c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0c ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref> <ref>PMID:20002452</ref> <ref>PMID:17236139</ref> <ref>PMID:19377476</ref>		[[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref> <ref>PMID:20002452</ref> <ref>PMID:17236139</ref> <ref>PMID:19377476</ref>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref> <ref>PMID:16322693</ref> <ref>PMID:16678110</ref> <ref>PMID:18593899</ref> <ref>PMID:18235224</ref> <ref>PMID:19801544</ref>	+	[[http://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/RBX1_MOUSE RBX1_MOUSE]] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation (By similarity). Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By similarity).<ref>PMID:12140560</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref> <ref>PMID:16322693</ref> <ref>PMID:16678110</ref> <ref>PMID:18593899</ref> <ref>PMID:18235224</ref> <ref>PMID:19801544</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 20:
	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 4a0c" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
		+	*[[Cullin\|Cullin]]
		+	*[[RING box protein\|RING box protein]]
	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]		*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
	== References ==		== References ==
Line 26:		Line 30:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Faty, M]]		[[Category: Faty, M]]
	[[Category: Fischer, E S]]		[[Category: Fischer, E S]]

OCA at 08:41, 21 December 2014

OCA — Sun, 21 Dec 2014 08:41:12 GMT

←Older revision		Revision as of 08:41, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4a0c~~\| ~~PDB~~=4a0c \| ~~SCENE~~= }}	+	==STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX==
-	===~~STRUCTURE OF THE CAND1~~-CUL4B-~~RBX1 COMPLEX~~===	+	<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution\|resolution]] 3.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_22118460}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A0C 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>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u6g\|1u6g]], [[4a0l\|4a0l]], [[4a0k\|4a0k]]</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=4a0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a0c RCSB], [http://www.ebi.ac.uk/pdbsum/4a0c PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref> <ref>PMID:20002452</ref> <ref>PMID:17236139</ref> <ref>PMID:19377476</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref> <ref>PMID:12504025</ref> <ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref> <ref>PMID:16322693</ref> <ref>PMID:16678110</ref> <ref>PMID:18593899</ref> <ref>PMID:18235224</ref> <ref>PMID:19801544</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). The DCAF DDB2 detects UV-induced pyrimidine dimers in the genome and facilitates nucleotide excision repair. We provide the molecular basis for DDB2 receptor-mediated cyclobutane pyrimidine dimer recognition in chromatin. The structures of the fully assembled DDB1-DDB2-CUL4A/B-RBX1 (CRL4(DDB2)) ligases reveal that the mobility of the ligase arm creates a defined ubiquitination zone around the damage, which precludes direct ligase activation by DNA lesions. Instead, the COP9 signalosome (CSN) mediates the CRL4(DDB2) inhibition in a CSN5 independent, nonenzymatic, fashion. In turn, CSN inhibition is relieved upon DNA damage binding to the DDB2 module within CSN-CRL4(DDB2). The Cockayne syndrome A DCAF complex crystal structure shows that CRL4(DCAF(WD40)) ligases share common architectural features. Our data support a general mechanism of ligase activation, which is induced by CSN displacement from CRL4(DCAF) on substrate binding to the DCAF.

-	~~==Disease==~~	+	The Molecular Basis of CRL4(DDB2/CSA) Ubiquitin Ligase Architecture, Targeting, and Activation.,Fischer ES, Scrima A, Bohm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, Iwai S, Gut H, Sugasawa K, Thoma NH Cell. 2011 Nov 23;147(5):1024-39. PMID:22118460<ref>PMID:22118460</ref>
-	~~[[http:~~/~~/www~~.~~uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation~~, ~~X-linked~~, ~~syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]].~~ A ~~syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature~~, ~~craniofacial dysmorphism~~, ~~small testes~~, ~~muscle wasting in lower legs~~, ~~kyphosis~~, ~~joint hyperextensibility~~, ~~pes cavus~~, ~~small feet~~, ~~and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment~~, ~~tremor~~, ~~seizures~~, ~~gait ataxia~~, ~~hyperactivity and decreased attention span~~.~~<ref>PMID~~:~~17273978</ref><ref>~~PMID:~~20002452</ref><ref>PMID:17236139</ref>~~<ref>PMID:~~19377476~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~//www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref><ref>PMID:12504025</ref><ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, ~~contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays~~ a ~~role as part~~ of the ~~E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage~~. ~~Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication~~. ~~Required for ubiquitination~~ of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<~~ref~~>~~PMID:14578910</ref><ref>PMID:16322693</ref><ref>PMID:16678110</ref><ref>PMID:18593899</ref><ref>PMID:18235224</ref><ref>PMID:19801544~~</~~ref~~>	+	</div>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~4a0c~~]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA].	+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:022118460</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Faty, M.]]	+	[[Category: Faty, M]]
-	[[Category: Fischer, E S.]]	+	[[Category: Fischer, E S]]
-	[[Category: Gut, H.]]	+	[[Category: Gut, H]]
-	[[Category: Scrima, A.]]	+	[[Category: Scrima, A]]
-	[[Category: Thoma, N H.]]	+	[[Category: Thoma, N H]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Dna damage repair]]		[[Category: Dna damage repair]]

OCA at 23:43, 24 March 2013

OCA — Sun, 24 Mar 2013 23:43:46 GMT

←Older revision		Revision as of 23:43, 24 March 2013
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-	[[Image:4a0c.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_4a0c", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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	{{STRUCTURE_4a0c\| PDB=4a0c \| SCENE= }}		{{STRUCTURE_4a0c\| PDB=4a0c \| SCENE= }}
-
	===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===		===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===
		+	{{ABSTRACT_PUBMED_22118460}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Defects in CUL4B are the cause of mental retardation, X-linked, syndromic, 15 (MRXS15) [MIM:[http://omim.org/entry/300354 300354]]. A syndromic form of X-linked mental retardation characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span.<ref>PMID:17273978</ref><ref>PMID:20002452</ref><ref>PMID:17236139</ref><ref>PMID:19377476</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22118460}}, adds~~ the ~~Publication Abstract to~~ the ~~page~~	+	[[http://www.uniprot.org/uniprot/CAND1_HUMAN CAND1_HUMAN]] Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.<ref>PMID:12504026</ref><ref>PMID:12504025</ref><ref>PMID:12609982</ref> [[http://www.uniprot.org/uniprot/CUL4B_HUMAN CUL4B_HUMAN]] Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8.<ref>PMID:14578910</ref><ref>PMID:16322693</ref><ref>PMID:16678110</ref><ref>PMID:18593899</ref><ref>PMID:18235224</ref><ref>PMID:19801544</ref>
-	(~~as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 22118460 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_22118460}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:022118460</ref><references group="xtra"/>	+	<ref group="xtra">PMID:022118460</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA at 07:02, 7 December 2011

OCA — Wed, 07 Dec 2011 07:02:46 GMT

←Older revision		Revision as of 07:02, 7 December 2011
Line 1:		Line 1:
-	[[Image:4a0c.~~jpg~~\|left\|200px]]	+	[[Image:4a0c.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===		===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22118460}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22118460 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22118460}}

	==About this Structure==		==About this Structure==
	[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA].		[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022118460</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA at 06:33, 30 November 2011

OCA — Wed, 30 Nov 2011 06:33:31 GMT

←Older revision		Revision as of 06:33, 30 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4a0c.jpg\|left\|200px]]

-	The ~~entry 4a0c~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4a0c", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_4a0c\| PDB=4a0c \| SCENE= }}

-	~~Authors: Scrima, A., Fischer, E.S., Faty, M., Gut, H., Thoma, N.H.~~	+	===STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX===

-	~~Description:~~ Structure ~~of the CAND1~~-~~CUL4B-RBX1 complex~~	+
		+	==About this Structure==
		+	[[4a0c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0C OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Mus musculus]]
		+	[[Category: Faty, M.]]
		+	[[Category: Fischer, E S.]]
		+	[[Category: Gut, H.]]
		+	[[Category: Scrima, A.]]
		+	[[Category: Thoma, N H.]]
		+	[[Category: Cell cycle]]
		+	[[Category: Dna damage repair]]
		+	[[Category: Ligase]]
		+	[[Category: Transcription]]
		+	[[Category: Ubiquitin]]

OCA at 06:18, 5 October 2011

OCA — Wed, 05 Oct 2011 06:18:31 GMT

←Older revision		Revision as of 06:18, 5 October 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4a0c is ON HOLD	+	The entry 4a0c is ON HOLD until Paper Publication

	Authors: Scrima, A., Fischer, E.S., Faty, M., Gut, H., Thoma, N.H.		Authors: Scrima, A., Fischer, E.S., Faty, M., Gut, H., Thoma, N.H.

	Description: Structure of the CAND1-CUL4B-RBX1 complex		Description: Structure of the CAND1-CUL4B-RBX1 complex