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Interacting selectively and non-covalently with a death domain of a protein. The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD bind each other forming oligomers. Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB. Interacting selectively and non-covalently with the Bcl-2 homology (BH) domain of a protein. Bcl-2-related proteins share homology in one to four conserved regions designated the Bcl-2 homology (BH) domains BH1, BH2, BH3 and BH4. These domains contribute at multiple levels to the function of these proteins in cell death and survival. Anti-apoptotic members of the Bcl-2 family have four BH domains (BH1-BH4). Pro-apoptotic members have fewer BH domains. Interacting selectively and non-covalently with the BH3 domain of a protein of the Bcl-2 family. The BH3 domain is a potent death domain and has an important role in protein-protein interactions and in cell death. Interacting selectively and non-covalently with a specific domain of a protein.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: BH3 domain binding
Acc: GO:0051434
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with the BH3 domain of a protein of the Bcl-2 family. The BH3 domain is a potent death domain and has an important role in protein-protein interactions and in cell death.
Proteins in PDR annotated with:
   This term: 7 [Search]
   Term or descendants: 7 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0051434 - BH3 domain binding (interactive image map)
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Created and Maintained by: Michael Riffle