Matches in DBpedia 2014 for { <http://dbpedia.org/resource/BAG_domain> ?p ?o. }
Showing items 1 to 36 of
36
with 100 items per page.
- BAG_domain abstract "In molecular biology, BAG domains are protein domains found in proteins which are modulators of chaperone activity, they bind to HSP70/HSC70 proteins and promote substrate release. The proteins have anti-apoptotic activity and increase the anti-cell death function of BCL-2 induced by various stimuli. BAG-1 binds to the serine/threonine kinase Raf-1 or Hsc70/Hsp70 in a mutually exclusive interaction. BAG-1 promotes cell growth by binding to and stimulating Raf-1 activity. The binding of Hsp70 to BAG-1 diminishes Raf-1 signalling and inhibits subsequent events, such as DNA synthesis, as well as arrests the cell cycle. BAG-1 has been suggested to function as a molecular switch that encourages cells to proliferate in normal conditions but become quiescent under a stressful environment .BAG-family proteins contain a single BAG domain, except for human BAG-5 which has four BAG repeats. The BAG domain is a conserved region located at the C terminus of the BAG-family proteins that binds the ATPase domain of Hsc70/Hsp70. The BAG domain is evolutionarily conserved, and BAG domain containing proteins have been described and/or proven in a variety of organisms including Mus musculus (Mouse), Xenopus spp., Drosophila spp., Bombyx mori (Silk moth), Caenorhabditis elegans, Saccharomyces cerevisiae (Baker's yeast), Schizosaccharomyces pombe (Fission yeast), and Arabidopsis thaliana (Mouse-ear cress).The BAG domain has 110-124 amino acids and is composed of three anti-parallel alpha-helices, each approximately 30-40 amino acids in length. The first and second helices interact with the serine/threonine kinase Raf-1 and the second and third helices are the sites of the BAG domain interaction with the ATPase domain of Hsc70/Hsp70. Binding of the BAG domain to the ATPase domain is mediated by both electrostatic and hydrophobic interactions in BAG-1 and is energy requiring.".
- BAG_domain symbol "BAG".
- BAG_domain thumbnail PDB_1hx1_EBI.jpg?width=300.
- BAG_domain wikiPageID "32158798".
- BAG_domain wikiPageRevisionID "590729325".
- BAG_domain caption "crystal structure of a bag domain in complex with the hsc70 atpase domain".
- BAG_domain hasPhotoCollection BAG_domain.
- BAG_domain interpro "IPR003103".
- BAG_domain name "BAG".
- BAG_domain pfam "PF02179".
- BAG_domain scop "1".
- BAG_domain smart "BAG".
- BAG_domain symbol "BAG".
- BAG_domain subject Category:Protein_families.
- BAG_domain type Abstraction100002137.
- BAG_domain type Family108078020.
- BAG_domain type Group100031264.
- BAG_domain type Organization108008335.
- BAG_domain type ProteinFamilies.
- BAG_domain type SocialGroup107950920.
- BAG_domain type Unit108189659.
- BAG_domain type YagoLegalActor.
- BAG_domain type YagoLegalActorGeo.
- BAG_domain type YagoPermanentlyLocatedEntity.
- BAG_domain type Biomolecule.
- BAG_domain type Protein.
- BAG_domain type BiologicalObject.
- BAG_domain comment "In molecular biology, BAG domains are protein domains found in proteins which are modulators of chaperone activity, they bind to HSP70/HSC70 proteins and promote substrate release. The proteins have anti-apoptotic activity and increase the anti-cell death function of BCL-2 induced by various stimuli. BAG-1 binds to the serine/threonine kinase Raf-1 or Hsc70/Hsp70 in a mutually exclusive interaction. BAG-1 promotes cell growth by binding to and stimulating Raf-1 activity.".
- BAG_domain label "BAG domain".
- BAG_domain sameAs m.0gx2blf.
- BAG_domain sameAs Q4834553.
- BAG_domain sameAs Q4834553.
- BAG_domain sameAs BAG_domain.
- BAG_domain wasDerivedFrom BAG_domain?oldid=590729325.
- BAG_domain depiction PDB_1hx1_EBI.jpg.
- BAG_domain isPrimaryTopicOf BAG_domain.