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Single-round and productive infection by HIV-1 can be attained by providing the PBj Vpx protein in trans using PBj-derived but not HIV-1-derived particles, the molecular basis for this specificity remains unknown.
What is the basis for this specificity?
The mechanistic basis for this specificity contextual remains to be determined.
Here we discuss what is known about halide selectivity for the different halogenases and describe what is currently understood about the basis for this specificity.
Most recently, the crystal structure of the polymerase in complex with a DNA promoter has revealed the structural basis for this specificity [ 1, 2].
However, Akirin-2 was required for the regulation of only a specific subset of LPS and IL-1 inducible genes (Goto et al, 2008), although the molecular basis for this specificity remained unclear.
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Here, we present two crystal structures of Tectonin 2 from the mushroom Laccaria bicolor in complex with methylated ligands, unraveling the molecular basis for this original specificity.
The structural basis for this partial specificity and the consensus sequence for the resolvase catalytic domain are still unclear.
Despite numerous studies aimed at uncovering a basis for this substrate specificity, it is still not perfectly clear how IKK only facilitates this chemistry.
In order to elucidate the molecular basis for this coenzyme specificity, we have performed a site-directed mutagenesis study on phenylacetone monooxygenase (PAMO) from Thermobifida fusca.
The crystal structure of this inhibitor (AR_F8) in complex with caspase-2 reveals the molecular basis for the specificity and, together with kinetic analyses, the allosteric mechanism of inhibition.
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