Literature summary for 2.3.2.31 extracted from

Tsai, Y.I.; Johansson, H.; Dixon, D.; Martin, S.; Chung, C.W.; Clarkson, J.; House, D.; Rittinger, K.
Single-domain antibodies as crystallization chaperones to enable structure-based inhibitor development for RBR E3 ubiquitin ligases (2020), Cell Chem. Biol., 27, 83-93.e9 .

Search for more literature for 2.3.2.31

Application

Application	Comment	Organism
analysis	co-crystal structure of HOIP RBR domain with single-domain antibody, use as a platform for soaking of ligands that target the active site cysteine of HOIP	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
cocrystal structure of HOIP RBR domain with single-domain antibody, use as a platform for soaking of ligands that target the active site cysteine of HOIP	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	single-domain antibodies can modulate the activity of the E3 ligase HOIP and facilitate crystallization of its catalytic RBR domain. Single domain antibodies may inhibit most, if not all, ubiquitin linear chain formation with both E2 enzymes UbcH5C and UbcH7 equally, one group of antibodies has a small effect on the observed activity with UbcH5C, but drastically slows down linear chain formation with UbcH7	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96EP0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[E2 ubiquitin-conjugating enzyme UbcH5C]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine	-	Homo sapiens	[E2 ubiquitin-conjugating enzyme UbcH5C]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine	-	?
[E2 ubiquitin-conjugating enzyme UBCH7]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine	-	Homo sapiens	[E2 ubiquitin-conjugating enzyme UBCH7]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine	-	?

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Release 2023.1 (January 2023)