1zy3

Structural model of complex of Bcl-w protein with Bid BH3-peptideStructural model of complex of Bcl-w protein with Bid BH3-peptide

Structural highlights 1zy3 is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1mk3 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements in both the peptide and protein components of the complex and led to the displacement and unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with a bound BID-BH3 peptide was determined using NMR spectroscopy and molecular docking. These studies confirmed that a region of 16 residues of the BID-BH3 peptide is responsible for its strong binding to BCL-w and BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with dodecylphosphocholine micelles were characterized and showed that the conformational change of BCL-w upon lipid binding occurred at the same time as the release and unfolding of the BH3 peptide. Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles.,Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:16475813 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bcl-2

spinqualitylabelsall models 1zy3, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image