Vaccinia virus N1L protein resembles a B cell lymphoma‐2 (Bcl‐2) family protein
- 1 January 2007
- journal article
- Published by Wiley in Protein Science
- Vol. 16 (1) , 118-124
- https://doi.org/10.1110/ps.062454707
Abstract
Poxviruses encode immuno-modulatory proteins capable of subverting host defenses. The poxvirus vaccinia expresses a small 14-kDa protein, N1L, that is critical for virulence. We report the crystal structure of N1L, which reveals an unexpected but striking resemblance to host apoptotic regulators of the B cell lymphoma-2 (Bcl-2) family. Although N1L lacks detectable Bcl-2 homology (BH) motifs at the sequence level, we show that N1L binds with high affinity to the BH3 peptides of pro-apoptotic Bcl-2 family proteins in vitro, consistent with a role for N1L in modulating host antiviral defenses.Keywords
This publication has 48 references indexed in Scilit:
- Myxoma Virus M11L Blocks Apoptosis through Inhibition of Conformational Activation of Bax at the MitochondriaJournal of Virology, 2006
- BCL-XL Dimerization by Three-dimensional Domain SwappingJournal of Molecular Biology, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Myxoma Virus M11L Prevents Apoptosis through Constitutive Interaction with BakJournal of Virology, 2004
- The victorin‐induced mitochondrial permeability transition precedes cell shrinkage and biochemical markers of cell death, and shrinkage occurs without loss of membrane integrityThe Plant Journal, 2004
- Cell Death: Critical Control PointsPublished by Elsevier ,2004
- XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron DensityJournal of Structural Biology, 1999
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Methods used in the structure determination of bovine mitochondrial F1 ATPaseActa Crystallographica Section D-Biological Crystallography, 1996
- Atomic Structures of the Human Immunophilin FKBP-12 Complexes with FK506 and RapamycinJournal of Molecular Biology, 1993