4jgh: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4jgh|  PDB=4jgh  |  SCENE=  }}
===Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5===
{{ABSTRACT_PUBMED_23897481}}


The entry 4jgh is ON HOLD until Paper Publication
==Function==
[[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.


Authors: Kim, Y.K., Kwak, M.J., Ku, B., Suh, H.Y., Joo, K., Lee, J., Jung, J.U., Oh, B.H.
==About this Structure==
[[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].  


Description: Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5
==Reference==
<ref group="xtra">PMID:023897481</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Joo, K.]]
[[Category: Jung, J U.]]
[[Category: Kim, Y K.]]
[[Category: Ku, B.]]
[[Category: Kwak, M J.]]
[[Category: Lee, J.]]
[[Category: Oh, B H.]]
[[Category: Suh, H Y.]]
[[Category: Cullin-ring e3 ubiquitin ligase]]
[[Category: Cytosol]]
[[Category: Ligase]]
[[Category: Ubiquitination]]

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