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The red ribbon symbolizes the global solidarity with people living with HIV/AIDS and the commitment to fight this disease. Here, the ribbon puzzle represents the HIV capsid assembly, which is essential for the integrity of the immature and mature virus particle. Individual capsid protein dimers form the puzzle pieces. Binding of a newly identified peptide inhibitor alters the pieces such that they cannot assemble into infectious particles. The peptide is thus a lead compound for a new class of HIV drugs. pp 671-677, pp 678-682; News and Views pp 638-639.
Two studies now explain why triplet DNA repeats tend to expand in the human genome, causing such severe hereditary neurological disorders as myotonic dystrophy and Huntington disease.
Two recent papers identify the first peptide inhibitor that binds to the structural protein of HIV-1, thereby blocking assembly of both immature and mature virus-like particles in vitro. These studies open the door to a strategy for the development of new therapies against the virus.
The recent crystal structure of tetra nucleosomes supports zigzag-based models of chromatin fiber structure. The next challenge is to understand the modulation of chromatin structure in the nucleus, characterized by variability in DNA, histones and non-histone components.
Two long-awaited structures of serine and tyrosine site-specific recombinases bound to DNA show how reactions that are basically the same can be carried out in surprisingly different ways.