Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The structure of the leucine-rich repeat variant protein reveals a novel fold consisting of alternating α- and 310-helices arranged in a right-handed superhelix that follows an N-terminal 4Fe:4S cluster-containing domain.
NMR resonances of backbone nuclei have been assigned for >95% of the residues in oxidized, substrate-free, perdeuterated 13C/15N-labelled MurB (347 residues). A novel approach utilizing minimum chemical shift changes was employed to localize the NADP+ binding site on MurB.
Buried water molecules play a pivotal structural and energetic role in mediating interactions between a bacterial oligopeptide transporter protein and its ligands.
Two very fast phases in the incipient folding of apomyoglobin are assigned to the formation of the first local and global structural elements of the protein.
The crystal structure of Plasmodium falciparum lactate dehydrogenase reveals a surprising shift in the position of the NADH cofactor that explains the unusual biochemical properties of this enzyme. There is also a distinctive surface cleft adjacent to the NADH binding pocket that forms an attractive target for inhibitor design.
NMR studies of the free and DNA-bound states of the lac represser headpiece show that formation of the hinge helix requires protein–protein interactions and occurs only when the represser binds to the full lac operator.
Rapid (millisecond) far-UV circular dichroism and fluorescence-monitored kinetic studies of the unfolding of barstar demonstrate the accumulation of a compact intermediate devoid of much secondary structure, before the rate limiting step in unfolding.
An aromatic hydrogen bond—an interaction between the π-electron cloud of an aromatic ring and a hydrogen-bond donor—can substitute for a conventional hydrogen bond in sequence-specific protein—DNA interactions and can contribute 0.5–1 kcal mol−1 to binding and 1–2 kcal mol−1 to specificity.
The crystal structure of ferredoxin from Sulfolobus species strain 7 reveals a novel zinc-binding centre that may play an important role in stabilizing the protein and may be common to thermoacidophilic archaeal ferredoxins.
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.
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.
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
Estrogenic 17β-hydroxysteroid dehydrogenase may promote tumour growth in some breast carcinomas. The 2.3 Å structure of the human enzyme complexed with 17β-estradiol gives insight into the specificity of substrate binding.
The structure of the killer toxin from the yeast Williopsis mrakii (WmKT) corresponds to a so far hypothetical ancestral single-domain form of the βγ-crystallin structure type, although there is neither significant sequence homology nor coincidence of physiological functions.
α1-antichymotrypsin and Alzheimer's Aβ1–42 peptide appear to form a complex whose inferred structure suggests possible mechanisms for stimulation of Alzheimer's amyloid fibril formation.
The complex of Grb2-SH2 a BCR-Abl target peptide reveals that the peptide binds in a β-turn conformation; Trp 121 closes the binding site C-terminal to the phosphotyrosyl residue of the ligand and prevents it from assuming the expected extended conformation.
The structure of the N-terminal Ig-superfamily (IgSF) domain of NCAM has a high similarity with the intermediate set of Ig-like domains: the first domain of the vascular cell adhesion molecule (VCAM-1), the M5 domain in titin, and telokin.