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==STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX==
 
<StructureSection load='4a0c' size='340' side='right' caption='[[4a0c]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
==Structure of the CAND1-CUL4B-RBX1 complex==
<StructureSection load='4a0c' size='340' side='right'caption='[[4a0c]], [[Resolution|resolution]] 3.80&Aring;' 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 [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"><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]] 3.8&#8491;</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='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'>[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'>[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 ==
[[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> 
[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 ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, 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==
*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
*[[Cullin 3D structures|Cullin 3D structures]]
*[[Ring box protein 3D structures|Ring box protein 3D structures]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[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]]
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