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The SAND domain is present in many proteins that have been linked to chromatin-dependent transcriptional regulation and human disease, but their function has remained unknown. Recent studies have revealed that these modules are DNA binding domains of novel molecular structure.
Recent structural and cell biological studies show that the previously uncharacterized PX domain can bind both phospholipids and SH3 domains, suggesting that this module may play a critical role in coordinating membrane localization and protein complex assembly during cell signaling.
Recent structural studies suggest that not only the protein components but also the nature and location of the protein–protein interaction surfaces in basement membranes are highly conserved throughout the metazoa, suggesting that their precise ultrastructure will be invariant, and reflecting their critical role in early development.
The solution structure of a 5-methyl CpG dinucleotide in complex with the methyl-CpG binding domain from human MBD1 has provided new insights into how dinucleotide sequences are specifically recognized. Surprisingly, the methyl groups of the symmetrically methylated CpG sequence are each recognized in a distinct manner.
The high resolution structure of photsystem I reveals an asymmetry in the organization of its cofactors that has ramifications for the path of electron flow.
The in vitro selection of a ribozyme polymerase capable of catalyzing the faithful addition of up to 14 nucleotides to a series of noncovalently bound primers fills a niche in our understanding of the origins and evolution of life on Earth.
