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.

Proteins, Protein structure

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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.

Observations, DNA damage

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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.

United States, Science & research, Research, Apolipoproteins, Structure

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