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1zy3
From Proteopedia
| 1zy3, 10 NMR models () | |||||||||
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| Domains: | Bcl-2, BH4 | ||||||||
| Related: | 1mk3 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Structural model of complex of Bcl-w protein with Bid BH3-peptide
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.
About this Structure
1ZY3 is a 2 chains structure of sequences from Homo sapiens. Full experimental information is available from OCA.
Reference
- Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K. Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles. Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:16475813 doi:10.1021/bi052332s
Page seeded by OCA on Wed Feb 18 01:27:59 2009
