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Binding of measles virus hemagglutinin (MVH) to its cellular receptors triggers the activation of the fusion protein. The conformational changes of MVH upon receptor binding are now examined by locking the dimers using disulfide bonds, or by pulling on appropriately positioned hexahistidine tags. The results indicate that the dimer interface is pulled apart after receptor binding by twisting of the MVH heads.
The measles virus hemagglutinin (MVH) promotes viral attachment to host cells via interaction with signaling lymphocyte activation molecule (SLAM). Now the crystal structure of MVH head domain in complex with the distal domain of SLAM, together with functional work, reveals the details of this interaction and explains the effectiveness of the currently used vaccine.
In Drosophila, upregulation of genes on the single male X chromosome to match that from the two female Xs depends upon the MSL complex. The structures of complexes of MSL subunits now give insight into how the MOF histone acetyltransferase and MSL3 interact with MSL1, indicating that the latter acts as a scaffold to bring the complex together.
Understanding the structural dynamics of ribosomal components is key to understanding translation. The Z-DNA– and Z-RNA–binding domain from the human RNA editing enzyme ADAR1-L is now shown to bind to specific regions of ribosomal RNAs affecting translation, suggesting that these regions might at least transiently form Z-RNA structure not observed in crystal structures.
BiP is an Hsp70 chaperone in the endoplasmic reticulum (ER) and is crucial for protein folding and quality control. Using single-molecule and ensemble FRET, the conformational cycle of BiP has now been defined. Movement of the lid domain of BiP allows this chaperone to discriminate between peptide and protein substrates.
Telomere protein RAP1 is found in organisms from yeast to mammals, but has different functions. Now the crystal structures of the RAP1 C-terminus (RCT) with its different interacting partners, together with functional analyses, reveal a conserved interaction module used by mammalian and fission yeast Rap1 to interact with TRF2 and Taz1, respectively, to mediate telomere protection. In contrast, in budding yeast this module recruits Sir3 to telomeres to mediate transcriptional silencing.
