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Crystallization of RNA molecules can pose a challenge, and the U1A RNA binding protein has been used to facilitate the process. Now a different portable RNA sequence and a synthetic Fab are presented as tools for RNA structural determination. In addition to functioning as a crystallization chaperone, the Fab also serves as the search model to provide phase information.
Understanding genomic organization in three dimensions may be one key to understanding gene regulation. Through the combination of an advanced version of chromosome conformation capture technology and an integrated modeling platform, the structure of the α-globin locus in cells where it is silent is compared to that in cells with high α-globin expression.
Even though heterogeneous nuclear ribonucleoprotein C (hnRNP C) is among the most abundant proteins in the nucleus, its role in splicing has remained unresolved. Data obtained using a newly developed individual-nucleotide UV crosslinking and immunoprecipitation (iCLIP) technique, integrated with alternative splicing profiles, indicate how the position of hnRNP particles determines their effect on inclusion of alternative exons.
While the topological analysis of protein complexes by electron microscopy (EM) has developed in recent years, the exact position of single subunits within multisubunit complexes has been difficult. A new clonable peptide tag, which when attached to a target protein can recruit a structurally prominent label that is easily identifiable by EM, may help solve this problem.
Membrane proteins pose a huge challenge for structural analysis, but a new study reports the first NMR structure determination of a detergent-solubilized seven-helical transmembrane (7TM) protein, the phototaxis receptor sensory rhodopsin II. This case study may open the doors to similar solution NMR structures for other 7TM proteins.
SH2 domains are present in many proteins, and designing specific inhibitors has been a challenge. Now a monobody, based on a fibronectin type III domain scaffold, that targets the SH2 domain from Abl kinase is developed, with structural data revealing the basis of its specificity and functional work exploring its effects in vitro and in cells.
