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The X-ray structures of a lysozyme-complexed camel VH domain and an antigen-free llama VH domain reveal novel features that open up new possibilities for generating and engineering minimal antigen recognition units.
Spectroscopic evidence for tilting of smooth muscle, but not skeletal muscle, myosin heads when ADP dissociates suggests mechanisms for the adaptations of these muscle types for their specialized roles.
Electron microscopic image analysis and protein–DNA crosslinking show that DNA binds asymmetrically to the hexameric bacteriophage T7 gp4b helicase, and binds to only one or two subunits
A guanine-rich DNA oligomer (33 nucleotides), isolated by in vitro selection from a random-sequence DNA library, catalyses the insertion of copper(II) and zinc ions into mesoporphyrin IX.
The granulin/epithelin protein motif has an unusual structure consisting of a parallel stack of β-hairpins stapled together by six disulphide bonds. The new structure also contains a folding subdomain shared by small toxins, protease inhibitors as well as the EGF-like protein modules.
The 1.85 Å structure of an antigen-free llama heavy chain variable domain reveals a fold similarity to that of the classical immunoglobulin VHs, increased surface hydrophilicity of the side of the VH corresponding to that facing the VL domain in classical immunoglobulins, and alterations in the pattern of the CDRs.
Studies of a critical module in the ligand binding domain of the LDL receptor implicate a protein folding defect, coupled to a deficiency in calcium binding, as a major cause of familial hypercholesterolemia.
