Volume 4 Issue 10, October 1997

How does DNA in chromatin become accessible? The recent report of a nucleosome core particle structure offers insights into the dynamic interactions between chromatin and regulatory protein complexes.

Structural studies of translation are in a state of rapid progress. For eubacterial systems, low resolution images of whole ribosomes can be combined with high resolution structures of individual components. For eucaryotic systems, the first individual structures are just begining to emerge.

The structure of a conserved hairpin loop involved in peptidyl–tRNA recognition by SOS ribosomal subunits has been solved by NMR. The loop is closed by a novel G–C base pair and presents guanine residues for RNA recognition.

Amaranthus caudatus agglutinin contains a novel arrangement of four β-trefoil domains. The sugar-binding site provides specificity for the carcinoma-associated T-antigen disaccharide even when ‘masked’ by other sugars.

Spermadhesins, 12,000–14,000 M_r mammalian proteins, include lectins involved in sperm–egg binding and display a single CUB domain architecture. We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins, and bovine aSFP at 2.4 Å and 1.9 Å resolution respectively.

The 2.7 Å structure of the tetanus neurotoxin receptor binding fragment H_C reveals a jelly-roll domain and a β-trefoil domain. H_C retains the unique transport properties of the holotoxin and is capable of eliciting a protective immunological response against the full length holotoxin.

NK-lysin is the first representative of a family of sequence related proteins — saposins, surfactant-associated protein B, pore forming amoeba proteins, and domains of acid sphingomyelinase, acyloxyacylhydrolase and plant aspartic proteinases — for which a structure has been determined.

Staurosporine exhibits nanomolar IC₅₀ values against a wide range of protein kinases. The structure of a CDK2 strauroporine complex explains the tight binding of this inhibitor, and suggests features to be exploited in the design of specific inhibitors of CDKs.

A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.

The first NMR supplement contains reviews that discuss technological breakthroughs in using NMR for structure determination, as well as an online resource for NMR structural biologists