Proteases universally recognize beta strands in their active sites

Article Abstract:

An analysis of over 1500 three dimensional crystal and solution structures from the pdb of substrates, products, and inhibitors bound in the active sites of aspartic, serine, metallo, cysteine, and threonine endopeptidases is summarized. The results obtained indicate that aspartic, serine, cysteine, and metalloproteases bind to the extended beta-strand conformation of substrates, products and inhibitors of both peptidic and nonpeptidic origin.

Proteases, Enzymes, Crystals, Crystal structure, Enzyme structure-activity relationships

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Over one hundred peptide-activated G protein-coupled receptors recognize ligands with turn structure

Article Abstract:

The voluminous structural and/or activity evidence in support of a ligand turn shape being the likely recognition domain in G protein-coupled receptors (GPCR)-binding domains of ligands are assembled. A key factor for cell signaling via GPCRs, namely that peptide-activated GPCRs may recognize a broadly similar turn conformation or shape in their diverse peptidic ligand signals is demonstrated.

Radioligand assay

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Nonpeptidic ligands for peptide-activated G protein-coupled Receptors

Article Abstract:

The peptide-activated G protein-coupled receptors are coupled with nonpeptide ligands to enhance the affinity for a receptor. These are useful in the synthesis of low cost drugs with better bioavailability, stability.

Analysis, Chemical synthesis, Chemical properties, Hydrophobic effect

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