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5bxd

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Crystal structure of pentameric KCTD1 BTB domain form 2

Structural highlights

5bxd is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.796Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KCTD1_HUMAN Scalp-ear-nipple syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

KCTD1_HUMAN May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent.^[1] ^[2]

Publication Abstract from PubMed

Cullin3 (Cul3)-based ubiquitin E3 ligase complexes catalyze the transfer of ubiquitin from an E2 enzyme to target substrate proteins. In these assemblies, the C-terminal region of Cul3 binds Rbx1/E2~ubiquitin, while the N-terminal region interacts with various BTB domain proteins that serve as substrate adaptors. Previous crystal structures of the homodimeric BTB proteins KLHL3, KLHL11 and SPOP in complex with the N-terminal domain of Cul3 revealed the features required for Cul3 recognition in these proteins. A second class of BTB-domain containing proteins, the KCTD proteins, are also Cul3 substrate adaptors, but these do not share many of the previously identified determinants for Cul3 binding. We report the pentameric crystal structures of the KCTD1 and KCTD9 BTB domains, and identify plasticity in the KCTD1 rings. We find that the KCTD proteins 5, 6, 9, and 17 bind to Cul3 with high affinity, while the KCTD proteins 1 and 16 do not have detectable binding. Finally, we confirm the 5:5 assembly of KCTD9/Cul3 complexes by electron cryomicroscopy and provide a molecular rationale for BTB-mediated Cul3 binding specificity in the KCTD family.

Structural insights into KCTD protein assembly and Cullin3 recognition.,Ji AX, Chu A, Nielsen TK, Benlekbir S, Rubinstein JL, Prive GG J Mol Biol. 2015 Aug 31. pii: S0022-2836(15)00484-2. doi:, 10.1016/j.jmb.2015.08.019. PMID:26334369^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ding XF, Luo C, Ren KQ, Zhang J, Zhou JL, Hu X, Liu RS, Wang Y, Gao X, Zhang J. Characterization and expression of a human KCTD1 gene containing the BTB domain, which mediates transcriptional repression and homomeric interactions. DNA Cell Biol. 2008 May;27(5):257-65. doi: 10.1089/dna.2007.0662. PMID:18358072 doi:http://dx.doi.org/10.1089/dna.2007.0662
↑ Ding X, Luo C, Zhou J, Zhong Y, Hu X, Zhou F, Ren K, Gan L, He A, Zhu J, Gao X, Zhang J. The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation. J Cell Biochem. 2009 Feb 1;106(2):285-95. doi: 10.1002/jcb.22002. PMID:19115315 doi:http://dx.doi.org/10.1002/jcb.22002
↑ Ji AX, Chu A, Nielsen TK, Benlekbir S, Rubinstein JL, Prive GG. Structural insights into KCTD protein assembly and Cullin3 recognition. J Mol Biol. 2015 Aug 31. pii: S0022-2836(15)00484-2. doi:, 10.1016/j.jmb.2015.08.019. PMID:26334369 doi:http://dx.doi.org/10.1016/j.jmb.2015.08.019

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5bxd"

Categories: Homo sapiens | Large Structures | Chu A | Ji AX | Prive GG

@@ Line 1: / Line 1: @@
 ==Crystal structure of pentameric KCTD1 BTB domain form 2==
-<StructureSection load='5bxd' size='340' side='right' caption='[[5bxd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='5bxd' size='340' side='right'caption='[[5bxd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5bxd]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BXD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5bxd]] is a 5 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=5BXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BXD FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bxb|5bxb]], [[5bxh|5bxh]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.796&#8491;</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=5bxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bxd OCA], [http://pdbe.org/5bxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bxd RCSB], [http://www.ebi.ac.uk/pdbsum/5bxd PDBsum]</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=5bxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bxd OCA], [https://pdbe.org/5bxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bxd RCSB], [https://www.ebi.ac.uk/pdbsum/5bxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bxd ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/KCTD1_HUMAN KCTD1_HUMAN]] Scalp-ear-nipple syndrome. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/KCTD1_HUMAN KCTD1_HUMAN] Scalp-ear-nipple syndrome. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/KCTD1_HUMAN KCTD1_HUMAN]] May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent.<ref>PMID:18358072</ref> <ref>PMID:19115315</ref>
+[https://www.uniprot.org/uniprot/KCTD1_HUMAN KCTD1_HUMAN] May repress the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C to various extent.<ref>PMID:18358072</ref> <ref>PMID:19115315</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Chu, A]]
+[[Category: Homo sapiens]]
-[[Category: Ji, A X]]
+[[Category: Large Structures]]
-[[Category: Prive, G G]]
+[[Category: Chu A]]
-[[Category: Protein binding]]
+[[Category: Ji AX]]
+[[Category: Prive GG]]

5bxd

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Current revision

Crystal structure of pentameric KCTD1 BTB domain form 2

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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