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Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
It is suggested that the exclusion domain originates from a metallo‐protease inhibitor, characterized in people suffering from Haim–Munk and Papillon–Lefevre syndromes, suggests how they disrupt the fold and function of the enzyme.
Inositol hexakisphosphate kinase products contain diphosphate and triphosphate groups.
Revised Definition of Substrate Binding Sites of Papain-Like Cysteine Proteases
A review of kinetic and structural data has enabled us to reconsider the definition of substrate binding sites in papain-like cysteine proteases. Only three substrate binding sites, S2, S1 and S1',…
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.
Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors.
The structure confirms the role of residues His 110 and His 111 as the receptors of a peptidic substrate C-terminal carboxylic group and suggests that an epoxysuccinyl fragment can be used to extend binding into primed and nonprimed substrate binding sites of a papain-like cysteine protease.
Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases.
Metallophosphoesterases: structural fidelity with functional promiscuity.
The MPE superfamily is viewed as a set of proteins with a highly conserved structural core that allows embellishment to result in dramatic and niche-specific diversification of function.
Plasticity of Listeriolysin O Pores and its Regulation by pH and Unique Histidine
This work reports that the assembly of LLO pores is rapid and efficient irrespective of pH, and indicates significant plasticity of large β-barrel pores, controlled by environmental cues like pH.
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Mutagenic analysis and atomic force microscopy imaging suggest a mechanism for pore assembly for lysenin, which is relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria.
The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis.
- A. R. Shenoy, Nandini P Sreenath, M. Podobnik, M. Kovačevič, S. Visweswariah
- 6 December 2005
The Rv0805 protein hydrolyzes cAMP and cGMP in vitro, and overexpression in Mycobacterium smegmatis and E. coli reduces intracellular cAMP levels, and adds an additional level of complexity to cyclic nucleotide signaling in this organism.