Selected article for: "amino acid and binding region"

Author: Uversky, Vladimir N
Title: The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins
  • Document date: 2013_4_1
  • ID: 63gh2tg4_41
    Snippet: Glutamic acid-rich protein from cassava roots. Based on the analysis of changes in the cassava root proteome during physiological deterioration of cassava root after harvesting, it has been concluded that the glutamic acid-rich protein was one of the proteins that were upregulated after harvesting. 239 Cp190. Eukaryotic genomes contain a set of specific functional elements, chromatin insulators or boundary elements that regulate gene transcriptio.....
    Document: Glutamic acid-rich protein from cassava roots. Based on the analysis of changes in the cassava root proteome during physiological deterioration of cassava root after harvesting, it has been concluded that the glutamic acid-rich protein was one of the proteins that were upregulated after harvesting. 239 Cp190. Eukaryotic genomes contain a set of specific functional elements, chromatin insulators or boundary elements that regulate gene transcription by interfering with promoterenhancer communication. 240 In Drosophila melanogaster, the centrosome-associated zinc finger protein Cp190 protein (Cp190) is a component of the gypsy chromatin insulator complex, which is composed of Cp190, mod(mdg4) and su(Hw) and is required for the function of the gypsy chromatin insulator and other endogenous chromatin insulators organized by Su(Hw), CTCF the hippocampus and cerebral cortex of APP(E693Δ)-transgenic mice that are used as a model to study the pathological effects of Aβ oligomers in Alzheimer's disease. 228 ABRA. The acidic-basic repeat antigen (ABRA) is a 743-residues-long protein found in the vacuolar space surrounding merozoites in Plasmodium falciparum-infected erythrocytes, being localized in the parasitophorous vacuole and associated with the merozoite surface at the time of schizont rupture. 229 Due to its surface location, ABRA is one of the potential vaccine candidates against erythrocytic stages of malaria. 230 This protein is one of the antigens enriched in the clusters of merozoites formed with growth inhibitory immune serum and possesses chymotrypsinlike activity, 231 which can be inhibited with serine protease inhibitors such as chymostatin and phenyl methyl sulfonyl fluoride (PMSF). 232 It was shown that the N-terminal half of the protein is responsible for the protease activity, whereas the highly charged C-terminal part of the protein was not required for this activity. 232 Furthermore, the N-terminus contains an erythrocyte-binding domain located within the cysteine-rich N-proximal region of ABRA. 229 There are 111 glutamic acids and 108 lysines in ABRA, and in agreement with its name, the amino acid sequence of this protein is characterized by the presence of eight tandem repeats of [VT]-N-D-[ED]-[ED]-D (residues 226-273) and by a lysinerich C-terminal region (residues 672-721).

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