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An antiparallel DNA decanucleotide displays an unusual crystal structure in which each molecule is linked to a neighbour by base pairs between intertwined, looped strands. The structure suggests a model for the transcription bubble.
Measurement of proton uptake in the bacterial photosynthetic reaction centre indicates that the formation of has an electrostatic influence on the protonation of residue Glu-L212 some 17 Å distant from .
The crystal structure of the haemopexin-like C-terminal domain of gelatinase A reveals that it is a four-bladed β-propeller protein. The four blades are arranged around a channel-like opening in which Ca2+ and a Na-Cl+ion pair are bound.
The N-terminal domain of fibronectin undergoes factor XIIIa-catalysed crosslinking to fibrin, bacteria and collagen. The reactive glutamine residue is in an extended, random coil ‘tail’ of about 18 residues that would be accessible for crosslinking.
Crystal structures of target peptide bound Ca2+-calmodulin linker helix mutants with the helix shortened by two or three residues, or replaced by the longer troponin C central helix, show that the major calmodulin-target structure is preserved at the expense of linker conformation.
The structure of peptide N-AcYTLDADF when bound to the large subunit of mouse ribonucleotide reductase has been elucidated by transfer NOE. This structure suggests a general design for type 1 RR inhibitors.
The biologically active carboxy-terminal peptide of the G-protein receptor, rhodopsin, forms a compact structure, suggesting that it is a structural domain in this integral membrane protein. The disposition of serines explains receptor kinase specificity.
Two DNA-RNA chimers, complexed with DNA minor groove binding drugs, have been observed to adopt the B-form conformation for the first time. Thus, the RNA duplex may assume the B-DNA conformation when interacting with drugs, peptides or proteins.
Electron crystallography of frozen-hydrated two-dimensional crystals of deglycosylated human erythrocyte CHIP28 reveals an aqueous vestibule in each monomer leading to the water-selective channel that is enclosed by multiple transmembrane α-helices.
Computer modelling of the antithrombin III–heparin–thrombin complex inspired the synthesis of novel glycoconjugates, whose factor Xa and thrombin inhibitory activites can be adjusted in a rational way, leading to anticoagulants with unprecedented characteristics.
We have predicted a structure for the three A domains of blood coagulation factor VIII by virtue of their homology to blue copper-binding proteins. This structure, consisting of six β-barrels, is arranged in a triangular configuration with a single type II copper-binding site linking the A1 and A3 domains.
Amino-acid sequence comparison and tertiary structure modelling suggest a structure for type I DNA methyltransferases and an evolutionary link to type II DNA methyltransferases.
Comparison of the position of the haem-ligating methionine in different class I cytochromes c raises issues about the use of this methionine in sequence alignment in this family of proteins.
Application of the double autocorrelation technique to the published nucleosome database allows the periodical distribution of CC and AA dinucleotides along the nucleosomal DNA to be seen; periods of CC and AA distributions are clearly visualized at about 10 base pairs.
Examination of FK506, cyclosporin and rapamycin has revealed that the surface loops involved in molecular recognition may need to be rigid as well as hydrophobic.