1DDB

STRUCTURE OF MOUSE BID, NMR, 20 STRUCTURES

Summary for 1DDB

• Entry DOI: 10.2210/pdb1ddb/pdb
• Descriptor: PROTEIN (BID) (1 entity in total)
• Functional Keywords: apoptosis, programmed cell death, bcl-2 family, bh3 domain
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: P70444
• Total number of polymer chains: 1
• Total formula weight: 21974.63

Authors

Mcdonnell, J.M.,Fushman, D.,Milliman, C.,Korsmeyer, S.J.,Cowburn, D. (deposition date: 1999-02-19, release date: 1999-08-30, Last modification date: 2023-12-27)

Primary citation

McDonnell, J.M.,Fushman, D.,Milliman, C.L.,Korsmeyer, S.J.,Cowburn, D.
Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists.
Cell(Cambridge,Mass.), 96:625-634, 1999

PubMed Abstract: Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization.

PubMed: 10089878
DOI: 10.1016/S0092-8674(00)80573-5

Experimental method

SOLUTION NMR