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Ubiquitin
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<StructureSection load='' size='340' side='right' caption='Human ubiquitin (green) complex with ubiquitin-conjugating enzyme E2 (deep sky blue), [[3k9p]]' scene='41/417541/Cv/3' > | <StructureSection load='' size='340' side='right' caption='Human ubiquitin (green) complex with ubiquitin-conjugating enzyme E2 (deep sky blue), [[3k9p]]' scene='41/417541/Cv/3' > | ||
== Function == | == Function == | ||
| - | [[Ubiquitin]] (UBB) is found in almost all cells. It binds to proteins tagging them for destruction in the proteasome. UBB is activated by the UBB-activating enzymes E1, E2 and E3. UBB+1 is a frameshifted mutant of UBB observed in several diseases. A dimer of UBB (DiUBB) is formed by linkage of K48 to the C-terminus of a second UBB molecule. At least 4 UBB molecules are needed to tag a protein for the proteasome<ref>PMID:9759494</ref>. <scene name='41/417541/Cv/ | + | [[Ubiquitin]] (UBB) is found in almost all cells. It binds to proteins tagging them for destruction in the proteasome. UBB is activated by the UBB-activating enzymes E1, E2 and E3. UBB+1 is a frameshifted mutant of UBB observed in several diseases. A dimer of UBB (DiUBB) is formed by linkage of K48 to the C-terminus of a second UBB molecule. At least 4 UBB molecules are needed to tag a protein for the proteasome<ref>PMID:9759494</ref>. <scene name='41/417541/Cv/4'>Human ubiquitin interactions with ubiquitin-conjugating enzyme E2</scene> ([[3k9p]]). For details see<br /> |
* [[Ubiquitin Structure & Function]]<br /> | * [[Ubiquitin Structure & Function]]<br /> | ||
* [[Ubiquitin salt bridge discussion]]<br /> | * [[Ubiquitin salt bridge discussion]]<br /> | ||
Revision as of 11:43, 7 October 2019
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3D Structures of Ubiquitin
Updated on 07-October-2019
References
- ↑ Hershko A, Ciechanover A. The ubiquitin system. Annu Rev Biochem. 1998;67:425-79. PMID:9759494 doi:http://dx.doi.org/10.1146/annurev.biochem.67.1.425
- ↑ Paul S. Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. Bioessays. 2008 Nov;30(11-12):1172-84. doi: 10.1002/bies.20852. PMID:18937370 doi:http://dx.doi.org/10.1002/bies.20852
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