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Structure and specificity of nuclear receptor-coactivator interactions.
TLDR
Biochemical and crystallographic analyses revealed that hormone binding leads to the formation of a hydrophobic groove within the ligand binding domain of the thyroid hormone receptor that interacts with an LxxLL motif-containing alpha-helix from GRIP1, a coactivator, suggesting that these common structural elements impart flexibility to combinatorial regulation, whereas side chains at the interface impart specificity.
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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
TLDR
It is argued that the conversion of alpha-helices into beta-sheets underlies the formation of PrPSc, and it is likely that this conformational transition is a fundamental event in the propagation of prions.
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A structural role for hormone in the thyroid hormone receptor
TLDR
A structural role for ligand is suggested, in establishing the active conformation of the receptor, that is likely to underlie hormonal regulation of gene expression for the nuclear receptors.
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Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
TLDR
Although kinesin and myosin have virtually no amino-acid sequence identity, and exhibit distinct enzymatic4–6 and motile7–10 properties, the results suggest that these two classes of mechanochemical enzymes evolved from a common ancestor and share a similar force-generating strategy.
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The design plan of kinesin motors.
TLDR
Structural features common to all kinesin motors, as well as specialized features that enable subfamilies of related motors to carry out specialized activities, are discussed.
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The family of glycogen phosphorylases: structure and function.
TLDR
The functional properties of rabbit muscle phosphorylases are reviewed and then compared to properties of phosphoryLases from other tissues and organisms, and Evolutionary relationships among phosphory lases as afforded by comparative analysis of proteins and gene sequences are discussed.
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Switch-based mechanism of kinesin motors
TLDR
Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.
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Structural Analyses Reveal Phosphatidyl Inositols as Ligands for the NR5 Orphan Receptors SF-1 and LRH-1
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Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.
TLDR
This classification allows the molecular mapping of residues from viral sequences onto related tertiary structures and precisely identifies amino acids that are strong determinants of specificity for both small and large viral cysteine proteases.
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Ca(2+)-regulated structural changes in troponin.
TLDR
It is shown that Anapoe, a detergent molecule, increases the contractile force of muscle fibers and binds specifically, together with the TnI switch helix, in a hydrophobic pocket of TnC upon activation by Ca ions.
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