Interface Forming Residues
Mostrando 1-12 de 33 artigos, teses e dissertações.
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1. Utilização de alinhamento estrutural de proteínas no estudo de Interface Forming Residues de proteína-quinases com inibidores protéicos.
Alinhamento estrutural de proteínas e análise de interação proteína-inibidor. As proteínas-quinases (PK) como alvo biológico. Três grupos de estruturas diferentes no domínio catalítico de PK. Superposição dos dados obtidos no alinhamento sequencial e estrutural.
Campinas: Embrapa Informática Agropecuária. Publicado em: 2011
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2. Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors.
Background: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider cat
BMC Structural Biology. Publicado em: 2011
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3. Anchor residues in protein–protein interactions
We show that the mechanism for molecular recognition requires one of the interacting proteins, usually the smaller of the two, to anchor a specific side chain in a structurally constrained binding groove of the other protein, providing a steric constraint that helps to stabilize a native-like bound intermediate. We identify the anchor residues in 39 protein�
National Academy of Sciences.
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4. Critical Factors Determining Dimerization of Human Antizyme Inhibitor*
Ornithine decarboxylase (ODC) is the first enzyme involved in polyamine biosynthesis, and it catalyzes the decarboxylation of ornithine to putrescine. ODC is a dimeric enzyme, whereas antizyme inhibitor (AZI), a positive regulator of ODC that is homologous to ODC, exists predominantly as a monomer and lacks decarboxylase activity. The goal of this paper was
American Society for Biochemistry and Molecular Biology.
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5. The crystal structure of staphylococcal enterotoxin type D reveals Zn2+-mediated homodimerization.
Bacterial superantigens, including the staphylococcal enterotoxins, are the most potent activators of T cells known and have been suggested as a causative factor in Gram-positive shock in humans. Staphylococcal enterotoxin D (SED) is dependent upon Zn2+ for high affinity interactions with MHC class II molecules and thus SED was co-crystallized with Zn2+. The
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6. Novel Vascular Endothelial Growth Factor D Variants with Increased Biological Activity*
Members of the vascular endothelial growth factor (VEGF) family play a pivotal role in angiogenesis and lymphangiogenesis. They are potential therapeutics to induce blood vessel formation in myocardium and skeletal muscle, when normal blood flow is compromised. Most members of the VEGF/platelet derived growth factor protein superfamily exist as covalently bo
American Society for Biochemistry and Molecular Biology.
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7. Conformation of a Bactericidal Domain of Puroindoline a: Structure and Mechanism of Action of a 13-Residue Antimicrobial Peptide
Puroindoline a, a wheat endosperm-specific protein containing a tryptophan-rich domain, was reported to have antimicrobial activities. We found that a 13-residue fragment of puroindoline a (FPVTWRWWKWWKG-NH2) (puroA) exhibits activity against both gram-positive and gram-negative bacteria. This suggests that puroA may be a bactericidal domain of puroindoline
American Society for Microbiology.
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8. Modulation of Bacillus thuringiensis Phosphatidylinositol-specific Phospholipase C Activity by Mutations in the Putative Dimerization Interface*
Cleavage of phosphatidylinositol (PI) to inositol 1,2-(cyclic)-phosphate (cIP) and cIP hydrolysis to inositol 1-phosphate by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C are activated by the enzyme binding to phosphatidylcholine (PC) surfaces. Part of this reflects improved binding of the protein to interfaces. However, crystallograph
American Society for Biochemistry and Molecular Biology.
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9. Analysis of the LAGLIDADG interface of the monomeric homing endonuclease I-DmoI
The general structural fold of the LAGLIDADG endonuclease family consists of two similar α/β domains (αββαββα) that assemble either as homodimers or monomers with the domains related by pseudo-two-fold symmetry. At the center of this symmetry is the closely packed LAGLIDADG two-helix bundle that forms the main inter- or intra-molecular contact regio
Oxford University Press.
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10. STING Millennium: a web-based suite of programs for comprehensive and simultaneous analysis of protein structure and sequence
STING Millennium Suite (SMS) is a new web-based suite of programs and databases providing visualization and a complex analysis of molecular sequence and structure for the data deposited at the Protein Data Bank (PDB). SMS operates with a collection of both publicly available data (PDB, HSSP, Prosite) and its own data (contacts, interface contacts, surface ac
Oxford University Press.
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11. Correlating protein footprinting with mutational analysis in the bacterial transcription factor σ54 (σN)
Protein footprints of the enhancer-dependent σ54 protein, upon binding the Escherichia coli RNA polymerase core enzyme or upon forming closed promoter complexes, identified surface-exposed residues in σ54 of potential functional importance at the interface between σ54 and core RNA polymerases (RNAP) or DNA. We have now characterised alanine and glycine su
Oxford University Press.
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12. Crystal structure of the complex between thrombin and the central “E” region of fibrin
Nonsubstrate interactions of thrombin with fibrin play an important role in modulating its procoagulant activity. To establish the structural basis for these interactions, we crystallized d-Phe-Pro-Arg-chloromethyl ketone-inhibited human thrombin in complex with a fragment, Eht, corresponding to the central region of human fibrin, and solved its structure at
National Academy of Sciences.