1q59 | pdb_00001q59

Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2

spinqualitylabelsall models 1q59 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1q59 is a 1 chain structure with sequence from Human gammaherpesvirus 4. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EAR_EBVB9 Prevents premature death of the host cell during virus production, which would otherwise reduce the amount of progeny virus. Acts as a host B-cell leukemia/lymphoma 2 (Bcl-2) homolog, and interacts with pro-apoptotic proteins to prevent mitochondria permeabilization, release of cytochrome c and subsequent apoptosis of the host cell. Publication Abstract from PubMed The three-dimensional structure of BHRF1, the Bcl-2 homolog from Epstein-Barr virus (EBV), has been determined by NMR spectroscopy. Although the overall structure is similar to other Bcl-2 family members, there are important structural differences. Unlike some of the other Bcl-2 family members, BHRF1 does not contain the prominent hydrophobic groove that mediates binding to pro-apoptotic family members. In addition, in contrast to the anti-apoptotic Bcl-2 proteins, BHRF1 does not bind tightly to peptides derived from the pro-apoptotic proteins Bak, Bax, Bik, and Bad. The lack of an exposed, pre-formed binding groove in BHRF1 and the lack of significant binding to peptides derived from pro-apoptotic family members that bind to other anti-apoptotic family members, suggest that the mechanism of the BHRF1 anti-apoptotic activity does not parallel that of cellular Bcl-x(L) or Bcl-2. Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2.,Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET J Mol Biol. 2003 Oct 3;332(5):1123-30. PMID:14499614 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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