4eoz - Revision history

OCA at 07:21, 28 September 2022

OCA — Wed, 28 Sep 2022 07:21:18 GMT

←Older revision		Revision as of 07:21, 28 September 2022
Line 1:		Line 1:

	==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain==		==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain==
-	<StructureSection load='4eoz' size='340' side='right' caption='[[4eoz]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='4eoz' size='340' side='right'caption='[[4eoz]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4eoz]] is a 4 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=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EOZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4eoz]] is a 4 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=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOZ FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CUL3, KIAA0617 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [https://pdbe.org/4eoz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [https://www.ebi.ac.uk/pdbsum/4eoz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoz 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=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [~~http~~://pdbe.org/4eoz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4eoz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoz ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/CUL3_HUMAN CUL3_HUMAN]] Pseudohypoaldosteronism type 2E. Defects in CUL3 are the cause of Pseudohypoaldosteronism type 2E (PHA2E) [MIM:[http://omim.org/entry/614496 614496]]. An autosomal dominant disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics.<ref>PMID:22266938</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SPOP_HUMAN SPOP_HUMAN]] Inhibits IPF1/PDX1 transactivation of established target promoters, such as insulin, may be by recruiting a repressor complex (By similarity). In complex with CUL3, involved in ubiquitination of BMI1, H2AFY and DAXX, and probably also in ubiquitination and proteasomal degradation of Gli2 or Gli3.<ref>PMID:14528312</ref> <ref>PMID:15897469</ref> <ref>PMID:16524876</ref> [[http://www.uniprot.org/uniprot/CUL3_HUMAN CUL3_HUMAN]] Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the susbstrate recognition component. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; possibly by mediating ubiquitination of SLC12A3/NCC. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition.<ref>PMID:10500095</ref> <ref>PMID:11311237</ref> <ref>PMID:15897469</ref> <ref>PMID:16524876</ref> <ref>PMID:17543862</ref> <ref>PMID:22358839</ref>	+	[[https://www.uniprot.org/uniprot/SPOP_HUMAN SPOP_HUMAN]] Inhibits IPF1/PDX1 transactivation of established target promoters, such as insulin, may be by recruiting a repressor complex (By similarity). In complex with CUL3, involved in ubiquitination of BMI1, H2AFY and DAXX, and probably also in ubiquitination and proteasomal degradation of Gli2 or Gli3.<ref>PMID:14528312</ref> <ref>PMID:15897469</ref> <ref>PMID:16524876</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Cullin\|Cullin]]	+	*[[Cullin 3D structures\|Cullin 3D structures]]
		+	*[[Speckle-type POZ protein 3D structures\|Speckle-type POZ protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Errington, W J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Prive, G G~~]]	+	[[Category: Errington WJ]]
-	[[Category: ~~E3 ubiquitin ligase]]~~	+	[[Category: Prive GG]]
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 02:50, 11 December 2016

OCA — Sun, 11 Dec 2016 02:50:13 GMT

←Older revision		Revision as of 02:50, 11 December 2016
Line 1:		Line 1:
		+
	==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain==		==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain==
	<StructureSection load='4eoz' size='340' side='right' caption='[[4eoz]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4eoz' size='340' side='right' caption='[[4eoz]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4eoz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EOZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4eoz]] is a 4 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=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EOZ FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), CUL3, KIAA0617 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CUL3, KIAA0617 ([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=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [http://www.ebi.ac.uk/pdbsum/4eoz 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=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [http://pdbe.org/4eoz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [http://www.ebi.ac.uk/pdbsum/4eoz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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 4eoz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cullin\|Cullin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Errington, W J]]		[[Category: Errington, W J]]
	[[Category: Prive, G G]]		[[Category: Prive, G G]]

OCA at 16:05, 9 December 2014

OCA — Tue, 09 Dec 2014 16:05:19 GMT

←Older revision		Revision as of 16:05, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4eoz.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain==
		+	<StructureSection load='4eoz' size='340' side='right' caption='[[4eoz]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4eoz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EOZ FirstGlance]. <br>
		+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CUL3, KIAA0617 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [http://www.ebi.ac.uk/pdbsum/4eoz PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CUL3_HUMAN CUL3_HUMAN]] Pseudohypoaldosteronism type 2E. Defects in CUL3 are the cause of Pseudohypoaldosteronism type 2E (PHA2E) [MIM:[http://omim.org/entry/614496 614496]]. An autosomal dominant disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics.<ref>PMID:22266938</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SPOP_HUMAN SPOP_HUMAN]] Inhibits IPF1/PDX1 transactivation of established target promoters, such as insulin, may be by recruiting a repressor complex (By similarity). In complex with CUL3, involved in ubiquitination of BMI1, H2AFY and DAXX, and probably also in ubiquitination and proteasomal degradation of Gli2 or Gli3.<ref>PMID:14528312</ref> <ref>PMID:15897469</ref> <ref>PMID:16524876</ref> [[http://www.uniprot.org/uniprot/CUL3_HUMAN CUL3_HUMAN]] Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the susbstrate recognition component. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; possibly by mediating ubiquitination of SLC12A3/NCC. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition.<ref>PMID:10500095</ref> <ref>PMID:11311237</ref> <ref>PMID:15897469</ref> <ref>PMID:16524876</ref> <ref>PMID:17543862</ref> <ref>PMID:22358839</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The E3 ligases recruit substrate proteins for targeted ubiquitylation. Recent insights into the mechanisms of ubiquitylation demonstrate that E3 ligases can possess active regulatory properties beyond those of a simple assembly scaffold. Here, we describe the dimeric structure of the E3 ligase adaptor protein SPOP (speckle-type POZ protein) in complex with the N-terminal domain of Cul3 at 2.4 A resolution. We find that SPOP forms large oligomers that can form heteromeric species with the closely related paralog SPOPL. In combination, SPOP and SPOPL (SPOP-like) form a molecular rheostat that can fine-tune E3 ubiquitin ligase activity by affecting the oligomeric state of the E3 complex. We propose that adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates.

-	~~{{STRUCTURE_4eoz\| PDB=4eoz \| SCENE= }}~~	+	Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.,Errington WJ, Khan MQ, Bueler SA, Rubinstein JL, Chakrabartty A, Prive GG Structure. 2012 Jul 3;20(7):1141-53. Epub 2012 May 24. PMID:22632832<ref>PMID:22632832</ref>

-	~~===Crystal structure~~ of the ~~SPOP BTB domain complexed with the Cul3 N-terminal domain===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_22632832}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4eoz]] is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOZ OCA].~~	+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Errington, W J.]]	+	[[Category: Errington, W J]]
-	[[Category: Prive, G G.]]	+	[[Category: Prive, G G]]
	[[Category: E3 ubiquitin ligase]]		[[Category: E3 ubiquitin ligase]]
	[[Category: Nucleus]]		[[Category: Nucleus]]
	[[Category: Protein binding]]		[[Category: Protein binding]]

OCA at 08:11, 9 January 2013

OCA — Wed, 09 Jan 2013 08:11:28 GMT

←Older revision		Revision as of 08:11, 9 January 2013
Line 1:		Line 1:
-	[[Image:4eoz.~~jpg~~\|left\|200px]]	+	[[Image:4eoz.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_4eoz", 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_4eoz\| PDB=4eoz \| SCENE= }}		{{STRUCTURE_4eoz\| PDB=4eoz \| SCENE= }}

	===Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain===		===Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain===

		+	{{ABSTRACT_PUBMED_22632832}}

	==About this Structure==		==About this Structure==

OCA at 06:06, 30 May 2012

OCA — Wed, 30 May 2012 06:06:09 GMT

←Older revision		Revision as of 06:06, 30 May 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4eoz.jpg\|left\|200px]]

-	The ~~entry 4eoz~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4eoz", 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_4eoz\| PDB=4eoz \| SCENE= }}

-	~~Authors: Prive, G.G., Errington, W.J.~~	+	===Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain===

-	~~Description: Crystal~~ structure ~~of the SPOP BTB domain complexed~~ with ~~the Cul3 N~~-~~terminal domain~~	+
		+	==About this Structure==
		+	[[4eoz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOZ OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Errington, W J.]]
		+	[[Category: Prive, G G.]]
		+	[[Category: E3 ubiquitin ligase]]
		+	[[Category: Nucleus]]
		+	[[Category: Protein binding]]

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

OCA — Wed, 25 Apr 2012 08:55:57 GMT

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

←Older revision

Revision as of 08:55, 25 April 2012

OCA: New page: '''Unreleased structure''' The entry 4eoz is ON HOLD Authors: Prive, G.G., Errington, W.J. Description: Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal doma...

OCA — Wed, 25 Apr 2012 08:55:56 GMT

New page: '''Unreleased structure''' The entry 4eoz is ON HOLD Authors: Prive, G.G., Errington, W.J. Description: Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal doma...

New page

'''Unreleased structure'''

The entry 4eoz is ON HOLD

Authors: Prive, G.G., Errington, W.J.

Description: Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain