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November 20, 2017

Articles in Acta Cryst F

Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii

We determined the crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii HB8 in complex with the cofactor by X-ray diffraction methods. The monomeric structure consists of a Rossmann-like fold (domain I) and a substrate binding domain (domain II). The cofactor binds at the interface between adjacent subunits.

by K. J. Pampa et al. at November 20, 2017 08:12 AM

Crystal structure of the second fibronectin type III (FN3) domain from human collagen α1 type XX

The crystal structure of a fibronectin type III domain from human collagen α1 type XX (residues Pro386–Pro466) was solved at 2.5 Å resolution.

by Zhao et al. at November 20, 2017 08:12 AM

November 18, 2017

Current papers in Acta Cryst F

Meditope–Fab interaction: threading the hole

Meditope, a cyclic 12-residue peptide, binds to a unique binding side between the light and heavy chains of the cetuximab Fab. In an effort to improve the affinity of the interaction, it was sought to extend the side chain of Arg8 in the meditope, a residue that is accessible from the other side of the meditope binding site, in order to increase the number of interactions. These modifications included an n-butyl and n-octyl extension as well as hydroxyl, amine and carboxyl substitutions. The atomic structures of the complexes and the binding kinetics for each modified meditope indicated that each extension threaded through the Fab `hole' and that the carboxyethylarginine substitution makes a favorable interaction with the Fab, increasing the half-life of the complex by threefold compared with the unmodified meditope. Taken together, these studies provide a basis for the design of additional modifications to enhance the overall affinity of this unique interaction.

by Williams, J.C. at November 18, 2017 12:00 AM