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{{STRUCTURE_4jgh|  PDB=4jgh  |  SCENE=  }}
==Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5==
===Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5===
<StructureSection load='4jgh' size='340' side='right' caption='[[4jgh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
{{ABSTRACT_PUBMED_23897481}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4jgh]] is a 4 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=4JGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JGH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CIS2, Homo sapiens, SOCS2, SSI2, STATI2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Mus musculus, Tceb2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), Mus musculus, Tceb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), CUL5, Homo sapiens, VACM1 ([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=4jgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jgh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jgh RCSB], [http://www.ebi.ac.uk/pdbsum/4jgh PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cullin-RING ubiquitin ligases are multisubunit complexes that ubiquitinate various proteins. Six different cullins encoded by the human genome selectively pair with different adaptors and substrate receptors. It is presently poorly understood how cullin-2 (Cul2) and cullin-5 (Cul5) associate specifically with their adaptor elongin BC and a SOCS-box-containing substrate receptor. Here, crystallographic and mutational analyses of a quaternary complex between the N-terminal half of Cul5, elongin BC and SOCS2 are reported. Cul5 interacts extensively with elongin BC via residues that are highly conserved in Cul2 but not in other cullins. Cul5 also interacts with SOCS2, but via only two residues, Pro184 and Arg186, which are located in the C-terminal part of the SOCS box called the Cul5 box. Pro184 makes a ring-to-ring interaction with Trp53 of Cul5, which is substituted by alanine in Cul2. This interaction is shown to contribute significantly to the overall binding affinity between Cul5 and SOCS2-elongin BC. This study provides structural bases underlying the specificity of Cul5 and Cul2 for elongin BC and their preferential association with Cul5 or Cul2 box-containing substrate receptors.


==Function==
Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes.,Kim YK, Kwak MJ, Ku B, Suh HY, Joo K, Lee J, Jung JU, Oh BH Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1587-97. doi:, 10.1107/S0907444913011220. Epub 2013 Jul 20. PMID:23897481<ref>PMID:23897481</ref>
[[http://www.uniprot.org/uniprot/CUL5_HUMAN CUL5_HUMAN]] Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) 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 functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAk2. Seems to be involved poteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a cell surface vasopressin receptor. [[http://www.uniprot.org/uniprot/SOCS2_HUMAN SOCS2_HUMAN]] SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. [[http://www.uniprot.org/uniprot/ELOC_MOUSE ELOC_MOUSE]] 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).  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. [[http://www.uniprot.org/uniprot/ELOB_MOUSE ELOB_MOUSE]] 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). 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.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4jgh]] is a 4 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=4JGH OCA].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:023897481</ref><references group="xtra"/><references/>
*[[Transcription factor SIII|Transcription factor SIII]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Joo, K.]]
[[Category: Joo, K]]
[[Category: Jung, J U.]]
[[Category: Jung, J U]]
[[Category: Kim, Y K.]]
[[Category: Kim, Y K]]
[[Category: Ku, B.]]
[[Category: Ku, B]]
[[Category: Kwak, M J.]]
[[Category: Kwak, M J]]
[[Category: Lee, J.]]
[[Category: Lee, J]]
[[Category: Oh, B H.]]
[[Category: Oh, B H]]
[[Category: Suh, H Y.]]
[[Category: Suh, H Y]]
[[Category: Cullin-ring e3 ubiquitin ligase]]
[[Category: Cullin-ring e3 ubiquitin ligase]]
[[Category: Cytosol]]
[[Category: Cytosol]]
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Ubiquitination]]
[[Category: Ubiquitination]]

Revision as of 15:44, 21 December 2014

Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5

Structural highlights

4jgh is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:CIS2, Homo sapiens, SOCS2, SSI2, STATI2 (Homo sapiens), Mus musculus, Tceb2 (Mus musculus), Mus musculus, Tceb1 (Mus musculus), CUL5, Homo sapiens, VACM1 (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

The cullin-RING ubiquitin ligases are multisubunit complexes that ubiquitinate various proteins. Six different cullins encoded by the human genome selectively pair with different adaptors and substrate receptors. It is presently poorly understood how cullin-2 (Cul2) and cullin-5 (Cul5) associate specifically with their adaptor elongin BC and a SOCS-box-containing substrate receptor. Here, crystallographic and mutational analyses of a quaternary complex between the N-terminal half of Cul5, elongin BC and SOCS2 are reported. Cul5 interacts extensively with elongin BC via residues that are highly conserved in Cul2 but not in other cullins. Cul5 also interacts with SOCS2, but via only two residues, Pro184 and Arg186, which are located in the C-terminal part of the SOCS box called the Cul5 box. Pro184 makes a ring-to-ring interaction with Trp53 of Cul5, which is substituted by alanine in Cul2. This interaction is shown to contribute significantly to the overall binding affinity between Cul5 and SOCS2-elongin BC. This study provides structural bases underlying the specificity of Cul5 and Cul2 for elongin BC and their preferential association with Cul5 or Cul2 box-containing substrate receptors.

Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes.,Kim YK, Kwak MJ, Ku B, Suh HY, Joo K, Lee J, Jung JU, Oh BH Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1587-97. doi:, 10.1107/S0907444913011220. Epub 2013 Jul 20. PMID:23897481[1]

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

See Also

References

  1. ↑ Kim YK, Kwak MJ, Ku B, Suh HY, Joo K, Lee J, Jung JU, Oh BH. Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1587-97. doi:, 10.1107/S0907444913011220. Epub 2013 Jul 20. PMID:23897481 doi:10.1107/S0907444913011220

4jgh, resolution 3.00Å

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