X-ray and NMR structure of human Bcl-x(sub L), an inhibitor of programmed cell death
Article Abstract:
A member of Bcl-2 family of proteins which regulate programed cell death, Bcl-x(sub L) contains two alpha-helices of about 30 angstroms. The two helices are surrounded by amphipathic helices. The two central helices are arranged in an antiparallel fashion and mostly contain hydrophobic residues. A kink in the helix alpha-6 at Pro 180 changes the helix direction. An irregular turn containing two glycines connects the C-terminal helix alpha-7 to alpha-6. Both X-ray crystallographic and NMR spectroscopic structures of the protein are similar and well defined.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
Mutations caught in the act
Article Abstract:
The proposal that disfavored tautomers are responsible for the mutations in the base substitutions is refuted. X-ray crystallography, NMR and enzyme kinetic studies reveal that mispaired sequences occur even when the bases are in the favored amino and keto forms. Mutations such as base substitutions and frameshifts occur in DNA due to DNA polymerase malfunction. The formation of base mispairs depends on the properties of the active site of the enzyme.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
The APOBEC-2 crystal structure and functional implications for the deaminase AID
Article Abstract:
The crystal structure of APOBEC-2 (APO2), which belongs to the family of apolipoprotein B messenger RNA-editing enzyme catalytic (APOBEC) polypeptides, is reported. The analysis has shown that activation-induced cytidine deaminase (AID) deamination activity is impaired by mutations predicted to interfere with oligomerization and substrate access, whereas the structure has shown how mutations in patients with hyper-IgM-2 syndrome inactivate AID.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Three-dimensional structure of a tubulin-motor-protein complex. Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
- Abstracts: Fas(CD95)/FasL interactions required for programmed cell death after T-cell activation. Protection against Fas-dependent Th1-mediated apoptosis by antigen receptor engagement in B cells
- Abstracts: A BDNF autocrine loop in adult sensory neurons prevents cell death. Neuron saving schemes
- Abstracts: Greek earthquake stirs controversy over claims for prediction method. Court charges open split in Greek earthquake experts
- Abstracts: Activation of human aortic smooth-muscle cells is inhibited by PPAR-alpha but not by PPAR-gamma activators. Transient increase in obese gene expression after food intake or insulin administration