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2a26

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<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=2a26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a26 RCSB], [http://www.ebi.ac.uk/pdbsum/2a26 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=2a26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a26 RCSB], [http://www.ebi.ac.uk/pdbsum/2a26 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/CYBP_HUMAN CYBP_HUMAN]] May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).<ref>PMID:16085652</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 18:04, 24 December 2014

Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein

2a26, resolution 1.20Å

Drag the structure with the mouse to rotate

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